TY  - JOUR
AU  - Zarić, Božidarka L.
AU  - Jovanović, Vesna B.
AU  - Stojanović, Srđan Đ.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1140
AB  - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. (C) 2010 Elsevier Ltd. All rights reserved.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Theoretical Biology
T1  - Non-covalent interactions across subunit interfaces in Sm proteins
VL  - 271
IS  - 1
SP  - 18
EP  - 26
DO  - 10.1016/j.jtbi.2010.11.025
ER  - 

@article{
author = "Zarić, Božidarka L. and Jovanović, Vesna B. and Stojanović, Srđan Đ.",
year = "2011",
abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. (C) 2010 Elsevier Ltd. All rights reserved.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Theoretical Biology",
title = "Non-covalent interactions across subunit interfaces in Sm proteins",
volume = "271",
number = "1",
pages = "18-26",
doi = "10.1016/j.jtbi.2010.11.025"
}

Zarić, B. L., Jovanović, V. B.,& Stojanović, S. Đ.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology
Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26.
https://doi.org/10.1016/j.jtbi.2010.11.025

Zarić BL, Jovanović VB, Stojanović SĐ. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26.
doi:10.1016/j.jtbi.2010.11.025 .

Zarić, Božidarka L., Jovanović, Vesna B., Stojanović, Srđan Đ., "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26,
https://doi.org/10.1016/j.jtbi.2010.11.025 . .

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Stanić, Dragana
AU  - Stojadinović, Marija M.
AU  - Ognjenović, Jana
AU  - Mihajlovic, Luka
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1137
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
VL  - 125
IS  - 1
SP  - 84
EP  - 91
DO  - 10.1016/j.foodchem.2010.08.040
ER  - 

@article{
author = "Tantoush, Ziyad and Stanić, Dragana and Stojadinović, Marija M. and Ognjenović, Jana and Mihajlovic, Luka and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics",
volume = "125",
number = "1",
pages = "84-91",
doi = "10.1016/j.foodchem.2010.08.040"
}

Tantoush, Z., Stanić, D., Stojadinović, M. M., Ognjenović, J., Mihajlovic, L., Atanasković-Marković, M.,& Ćirković-Veličković, T.. (2011). Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry
Elsevier Sci Ltd, Oxford., 125(1), 84-91.
https://doi.org/10.1016/j.foodchem.2010.08.040

Tantoush Z, Stanić D, Stojadinović MM, Ognjenović J, Mihajlovic L, Atanasković-Marković M, Ćirković-Veličković T. Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry. 2011;125(1):84-91.
doi:10.1016/j.foodchem.2010.08.040 .

Tantoush, Ziyad, Stanić, Dragana, Stojadinović, Marija M., Ognjenović, Jana, Mihajlovic, Luka, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics" in Food Chemistry, 125, no. 1 (2011):84-91,
https://doi.org/10.1016/j.foodchem.2010.08.040 . .

TY  - JOUR
AU  - Burazer, Lidija M.
AU  - Milovanovic, K.
AU  - Milovanovic, M.
AU  - Vučković, O.
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1152
AB  - House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Medical and Veterinary Entomology
T1  - Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population
VL  - 25
IS  - 1
SP  - 77
EP  - 83
DO  - 10.1111/j.1365-2915.2010.00906.x
ER  - 

@article{
author = "Burazer, Lidija M. and Milovanovic, K. and Milovanovic, M. and Vučković, O. and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija",
year = "2011",
abstract = "House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Medical and Veterinary Entomology",
title = "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population",
volume = "25",
number = "1",
pages = "77-83",
doi = "10.1111/j.1365-2915.2010.00906.x"
}

Burazer, L. M., Milovanovic, K., Milovanovic, M., Vučković, O., Ćirković-Veličković, T.,& Gavrović-Jankulović, M.. (2011). Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology
Wiley-Blackwell Publishing, Inc, Malden., 25(1), 77-83.
https://doi.org/10.1111/j.1365-2915.2010.00906.x

Burazer LM, Milovanovic K, Milovanovic M, Vučković O, Ćirković-Veličković T, Gavrović-Jankulović M. Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology. 2011;25(1):77-83.
doi:10.1111/j.1365-2915.2010.00906.x .

Burazer, Lidija M., Milovanovic, K., Milovanovic, M., Vučković, O., Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population" in Medical and Veterinary Entomology, 25, no. 1 (2011):77-83,
https://doi.org/10.1111/j.1365-2915.2010.00906.x . .

TY  - JOUR
AU  - Stojanović, Marijana M.
AU  - Živković, Irena
AU  - Petrusic, Vladimir Z.
AU  - Kosec, Dusko J.
AU  - Dimitrijevic, Rajna D.
AU  - Jankov, Ratko M.
AU  - Dimitrijevic, Ljijana A.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1043
AB  - Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved
PB  - Elsevier Science Bv, Amsterdam
T2  - International Immunopharmacology
T1  - In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma
VL  - 10
IS  - 1
SP  - 120
EP  - 129
DO  - 10.1016/j.intimp.2009.10.007
ER  - 

@article{
author = "Stojanović, Marijana M. and Živković, Irena and Petrusic, Vladimir Z. and Kosec, Dusko J. and Dimitrijevic, Rajna D. and Jankov, Ratko M. and Dimitrijevic, Ljijana A. and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "International Immunopharmacology",
title = "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma",
volume = "10",
number = "1",
pages = "120-129",
doi = "10.1016/j.intimp.2009.10.007"
}

Stojanović, M. M., Živković, I., Petrusic, V. Z., Kosec, D. J., Dimitrijevic, R. D., Jankov, R. M., Dimitrijevic, L. A.,& Gavrović-Jankulović, M.. (2010). In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology
Elsevier Science Bv, Amsterdam., 10(1), 120-129.
https://doi.org/10.1016/j.intimp.2009.10.007

Stojanović MM, Živković I, Petrusic VZ, Kosec DJ, Dimitrijevic RD, Jankov RM, Dimitrijevic LA, Gavrović-Jankulović M. In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology. 2010;10(1):120-129.
doi:10.1016/j.intimp.2009.10.007 .

Stojanović, Marijana M., Živković, Irena, Petrusic, Vladimir Z., Kosec, Dusko J., Dimitrijevic, Rajna D., Jankov, Ratko M., Dimitrijevic, Ljijana A., Gavrović-Jankulović, Marija, "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma" in International Immunopharmacology, 10, no. 1 (2010):120-129,
https://doi.org/10.1016/j.intimp.2009.10.007 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Obradovic, A.
AU  - Spasic, M.
AU  - Plecas-Solarovic, B.
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/108
AB  - Food allergens must exhibit sufficient gastrointestinal stability to reach the intestinal mucosa where absorption and sensitization can occur. Therefore, investigation of protein stability within the gastrointestinal tract may provide a prospective test for the allergenic potential of novel proteins. The aim of this work was to examine the effect of the fruit matrix and purified pectin on the digestion in vivo of kiwifruit allergens in the rat gastrointestinal system. The major kiwi allergen, Act d 2, was quantified in several compartments of the gastrointestinal tract by a monoclonal antibody-based ELISA. Protein intactness was demonstrated by immunoblot. Under conditions of complex food digestion in vivo, a pepsin-labile protein survived passage from the stomach to the caecum during a 3-h period. Decay of Act d 2 in the rat gut exhibited an exponential pattern. Ingestion of kiwifruit was followed by a decrease in both total and specific pepsin activity. When purified, Act d 2 allergen was consumed together with pure apple pectin; both gastric acidity as well as specific and total pepsin activity declined and thus protected 23% of the ingested allergen from digestion for 90 min. In conclusion, ingestion of pectin-rich fruits and particularly pectin supplements may have a protective action on pepsin-labile allergens and prolong their survival in both gastric and duodenal juices, enabling efficient uptake and presentation to the immune system. © Springer Science+Business Media, LLC 2010.
T2  - Food Digestion
T1  - In vivo digestion of a thaumatin-like kiwifruit protein in rats
VL  - 1
IS  - 1-2
SP  - 5
EP  - 13
DO  - 10.1007/s13228-010-0001-2
ER  - 

@article{
author = "Polović, Natalija and Obradovic, A. and Spasic, M. and Plecas-Solarovic, B. and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Food allergens must exhibit sufficient gastrointestinal stability to reach the intestinal mucosa where absorption and sensitization can occur. Therefore, investigation of protein stability within the gastrointestinal tract may provide a prospective test for the allergenic potential of novel proteins. The aim of this work was to examine the effect of the fruit matrix and purified pectin on the digestion in vivo of kiwifruit allergens in the rat gastrointestinal system. The major kiwi allergen, Act d 2, was quantified in several compartments of the gastrointestinal tract by a monoclonal antibody-based ELISA. Protein intactness was demonstrated by immunoblot. Under conditions of complex food digestion in vivo, a pepsin-labile protein survived passage from the stomach to the caecum during a 3-h period. Decay of Act d 2 in the rat gut exhibited an exponential pattern. Ingestion of kiwifruit was followed by a decrease in both total and specific pepsin activity. When purified, Act d 2 allergen was consumed together with pure apple pectin; both gastric acidity as well as specific and total pepsin activity declined and thus protected 23% of the ingested allergen from digestion for 90 min. In conclusion, ingestion of pectin-rich fruits and particularly pectin supplements may have a protective action on pepsin-labile allergens and prolong their survival in both gastric and duodenal juices, enabling efficient uptake and presentation to the immune system. © Springer Science+Business Media, LLC 2010.",
journal = "Food Digestion",
title = "In vivo digestion of a thaumatin-like kiwifruit protein in rats",
volume = "1",
number = "1-2",
pages = "5-13",
doi = "10.1007/s13228-010-0001-2"
}

Polović, N., Obradovic, A., Spasic, M., Plecas-Solarovic, B., Gavrović-Jankulović, M.,& Ćirković-Veličković, T.. (2010). In vivo digestion of a thaumatin-like kiwifruit protein in rats. in Food Digestion, 1(1-2), 5-13.
https://doi.org/10.1007/s13228-010-0001-2

Polović N, Obradovic A, Spasic M, Plecas-Solarovic B, Gavrović-Jankulović M, Ćirković-Veličković T. In vivo digestion of a thaumatin-like kiwifruit protein in rats. in Food Digestion. 2010;1(1-2):5-13.
doi:10.1007/s13228-010-0001-2 .

Polović, Natalija, Obradovic, A., Spasic, M., Plecas-Solarovic, B., Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, "In vivo digestion of a thaumatin-like kiwifruit protein in rats" in Food Digestion, 1, no. 1-2 (2010):5-13,
https://doi.org/10.1007/s13228-010-0001-2 . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Milovanovic, Mina
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Hoffmann-Sommergruber, Karin
AU  - Knulst, Andre C.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1068
AB  - Kiwifruit has become a frequent cause of fruit allergy in the recent years. The molecular basis of type I hypersensitivity to kiwifruit is attributed to 11 IUIS allergens, with Act d 1, Act d 2 and Act d 5 characterized in extenso. Evaluation of the allergenic properties of Act d 4, a cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa) was performed in this study. Identity of the purified glycoprotein was determined by Edman degradation and by mass fingerprint whereby more than 90% of the primary structure of the mature kiwifruit cystatin was confirmed. Using MALDI TOF analysis, molecular masses of 10902.5 and 11055.2 Da were detected for Act d 4, respectively. Positive skin prick reactivity with Act d 4 was induced in three kiwifruit allergic patients, as well as the upregulation of CD63 and CD203c molecules in the basophile activation assay. The IgE reactivity was detected in dot blot analysis while Western blot analysis was negative using sera from six kiwifruit patients, suggesting the presence of conformational IgE epitopes on the Act d 4 molecule. As activator of effector cells in type I hypersensitivity Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Molecular Nutrition and Food Research
T1  - Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy
VL  - 54
IS  - 3
SP  - 373
EP  - 380
DO  - 10.1002/mnfr.200900035
ER  - 

@article{
author = "Popović, Milica M. and Milovanovic, Mina and Burazer, Lidija M. and Vučković, Olga and Hoffmann-Sommergruber, Karin and Knulst, Andre C. and Lindner, Buko and Petersen, Arnd and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Kiwifruit has become a frequent cause of fruit allergy in the recent years. The molecular basis of type I hypersensitivity to kiwifruit is attributed to 11 IUIS allergens, with Act d 1, Act d 2 and Act d 5 characterized in extenso. Evaluation of the allergenic properties of Act d 4, a cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa) was performed in this study. Identity of the purified glycoprotein was determined by Edman degradation and by mass fingerprint whereby more than 90% of the primary structure of the mature kiwifruit cystatin was confirmed. Using MALDI TOF analysis, molecular masses of 10902.5 and 11055.2 Da were detected for Act d 4, respectively. Positive skin prick reactivity with Act d 4 was induced in three kiwifruit allergic patients, as well as the upregulation of CD63 and CD203c molecules in the basophile activation assay. The IgE reactivity was detected in dot blot analysis while Western blot analysis was negative using sera from six kiwifruit patients, suggesting the presence of conformational IgE epitopes on the Act d 4 molecule. As activator of effector cells in type I hypersensitivity Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Molecular Nutrition and Food Research",
title = "Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy",
volume = "54",
number = "3",
pages = "373-380",
doi = "10.1002/mnfr.200900035"
}

Popović, M. M., Milovanovic, M., Burazer, L. M., Vučković, O., Hoffmann-Sommergruber, K., Knulst, A. C., Lindner, B., Petersen, A., Jankov, R. M.,& Gavrović-Jankulović, M.. (2010). Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Molecular Nutrition and Food Research
Wiley-V C H Verlag Gmbh, Weinheim., 54(3), 373-380.
https://doi.org/10.1002/mnfr.200900035

Popović MM, Milovanovic M, Burazer LM, Vučković O, Hoffmann-Sommergruber K, Knulst AC, Lindner B, Petersen A, Jankov RM, Gavrović-Jankulović M. Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Molecular Nutrition and Food Research. 2010;54(3):373-380.
doi:10.1002/mnfr.200900035 .

Popović, Milica M., Milovanovic, Mina, Burazer, Lidija M., Vučković, Olga, Hoffmann-Sommergruber, Karin, Knulst, Andre C., Lindner, Buko, Petersen, Arnd, Jankov, Ratko M., Gavrović-Jankulović, Marija, "Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy" in Molecular Nutrition and Food Research, 54, no. 3 (2010):373-380,
https://doi.org/10.1002/mnfr.200900035 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1126
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
VL  - 54
IS  - 9
SP  - 1273
EP  - 1284
DO  - 10.1002/mnfr.200900184
ER  - 

@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vučković, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
volume = "54",
number = "9",
pages = "1273-1284",
doi = "10.1002/mnfr.200900184"
}

Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vučković, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley-V C H Verlag Gmbh, Weinheim., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184

Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vučković O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184 .

Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vučković, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 . .

TY  - JOUR
AU  - Dimitrijevic, Rajna
AU  - Jadranin, Milka
AU  - Burazer, Lidija M.
AU  - Ostojić, Sanja B.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1051
AB  - The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T(m)) of 60.8 degrees C, calorimetric enthalpy (H(cal)) of 136.17 kcal/mol and van't Hoff enthalpy (H(VH)) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT). (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Evaluation of the thermal stability and digestibility of heterologously produced banana lectin
VL  - 120
IS  - 4
SP  - 1113
EP  - 1118
DO  - 10.1016/j.foodchem.2009.11.062
ER  - 

@article{
author = "Dimitrijevic, Rajna and Jadranin, Milka and Burazer, Lidija M. and Ostojić, Sanja B. and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T(m)) of 60.8 degrees C, calorimetric enthalpy (H(cal)) of 136.17 kcal/mol and van't Hoff enthalpy (H(VH)) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT). (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin",
volume = "120",
number = "4",
pages = "1113-1118",
doi = "10.1016/j.foodchem.2009.11.062"
}

Dimitrijevic, R., Jadranin, M., Burazer, L. M., Ostojić, S. B.,& Gavrović-Jankulović, M.. (2010). Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(4), 1113-1118.
https://doi.org/10.1016/j.foodchem.2009.11.062

Dimitrijevic R, Jadranin M, Burazer LM, Ostojić SB, Gavrović-Jankulović M. Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry. 2010;120(4):1113-1118.
doi:10.1016/j.foodchem.2009.11.062 .

Dimitrijevic, Rajna, Jadranin, Milka, Burazer, Lidija M., Ostojić, Sanja B., Gavrović-Jankulović, Marija, "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin" in Food Chemistry, 120, no. 4 (2010):1113-1118,
https://doi.org/10.1016/j.foodchem.2009.11.062 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Dobrijevic, Dragana
AU  - Jadranin, Milka
AU  - Blanusa, Milan
AU  - Vukmirica, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1095
AB  - BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms. (C) 2010 Society of Chemical Industry
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases
VL  - 90
IS  - 10
SP  - 1702
EP  - 1708
DO  - 10.1002/jsfa.4005
ER  - 

@article{
author = "Radosavljević, Jelena and Dobrijevic, Dragana and Jadranin, Milka and Blanusa, Milan and Vukmirica, Jelena and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms. (C) 2010 Society of Chemical Industry",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases",
volume = "90",
number = "10",
pages = "1702-1708",
doi = "10.1002/jsfa.4005"
}

Radosavljević, J., Dobrijevic, D., Jadranin, M., Blanusa, M., Vukmirica, J.,& Ćirković-Veličković, T.. (2010). Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 90(10), 1702-1708.
https://doi.org/10.1002/jsfa.4005

Radosavljević J, Dobrijevic D, Jadranin M, Blanusa M, Vukmirica J, Ćirković-Veličković T. Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture. 2010;90(10):1702-1708.
doi:10.1002/jsfa.4005 .

Radosavljević, Jelena, Dobrijevic, Dragana, Jadranin, Milka, Blanusa, Milan, Vukmirica, Jelena, Ćirković-Veličković, Tanja, "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases" in Journal of the Science of Food and Agriculture, 90, no. 10 (2010):1702-1708,
https://doi.org/10.1002/jsfa.4005 . .

TY  - JOUR
AU  - Burazer, Lidija M.
AU  - Milovanovic, Katarina
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1045
AB  - Allergen-specific immunotherapy with house dust mite (HDM) allergen extracts can effectively alleviate the symptoms of allergic rhinitis and asthma. The efficacy of the immunotherapeutic treatment is highly dependent on the quality of house dust mite vaccines. This study was performed to assess the stability of house dust mite allergen vaccines prepared for sublingual immunotherapy. Lyophilized Dermatophagoides pteronyssinus (Dpt) mite bodies were the starting material for the production of sublingual vaccines in four therapeutic concentrations. The stability of the extract for vaccine production, which was stored below 4 degrees C for one month, showed consistence in the protein profile in SDS PAGE. ELISA-inhibition showed that the potencies of Dpt vaccines during a 12 month period were to 65-80 % preserved at all analyzed therapeutic concentrations. This study showed that glycerinated Dpt vaccines stored at 4 degrees C preserved their IgE-binding potential during a 12 month period, implying their suitability for sublingual immunotherapeutic treatment of HDM allergy.
AB  - Alergen-specifična imunoterapija predstavlja postupak koji može da promeni tok bolesti kod alergijskog rinitisa i astme. Kvalitet vakcine pripremljene od kućnih grinja značajno utiče na efikasnost imunoterapeutskog tretmana. Ispitivanje je imalo za cilj procenu stabilnosti vakcine kućnih grinja namenjene za sublingvalnu imunoterapiju. Telo liofilozovanih Dermatophagoides pteronyssinus grinja (Dpt-grinja) upotrebljeno je kao polazni materijal za proizvodnju sublingvalne vakcine u 4 različita terapeutska razblaženja. Potentnost Dpt vakcina praćena ELISA-inhibicijom u 4 terapeutska razblaženja, nakon 12 meseci zadržan je u svim razblaženjima u opsegu 65-80%. Ispitivanje je pokazalo da glicerolom stabilizovane Dpt vakcine za subligvalnu imunoterapiju, uz čuvanje na 4°C zadržavaju alergeni potencijal ( gt 65%) nakon 12 meseci od njihove pripreme, i kao takve mogu se koristiti za tretman alergije na kućne grinje.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Stability evaluation of house dust mite vaccines for sublingual immunotherapy
T1  - Ispitivanje stabilnosti vakcine kućne prašine za sublingvalnu imunoterapiju
VL  - 75
IS  - 1
SP  - 19
EP  - 26
DO  - 10.2298/JSC1001019B
ER  - 

@article{
author = "Burazer, Lidija M. and Milovanovic, Katarina and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Allergen-specific immunotherapy with house dust mite (HDM) allergen extracts can effectively alleviate the symptoms of allergic rhinitis and asthma. The efficacy of the immunotherapeutic treatment is highly dependent on the quality of house dust mite vaccines. This study was performed to assess the stability of house dust mite allergen vaccines prepared for sublingual immunotherapy. Lyophilized Dermatophagoides pteronyssinus (Dpt) mite bodies were the starting material for the production of sublingual vaccines in four therapeutic concentrations. The stability of the extract for vaccine production, which was stored below 4 degrees C for one month, showed consistence in the protein profile in SDS PAGE. ELISA-inhibition showed that the potencies of Dpt vaccines during a 12 month period were to 65-80 % preserved at all analyzed therapeutic concentrations. This study showed that glycerinated Dpt vaccines stored at 4 degrees C preserved their IgE-binding potential during a 12 month period, implying their suitability for sublingual immunotherapeutic treatment of HDM allergy., Alergen-specifična imunoterapija predstavlja postupak koji može da promeni tok bolesti kod alergijskog rinitisa i astme. Kvalitet vakcine pripremljene od kućnih grinja značajno utiče na efikasnost imunoterapeutskog tretmana. Ispitivanje je imalo za cilj procenu stabilnosti vakcine kućnih grinja namenjene za sublingvalnu imunoterapiju. Telo liofilozovanih Dermatophagoides pteronyssinus grinja (Dpt-grinja) upotrebljeno je kao polazni materijal za proizvodnju sublingvalne vakcine u 4 različita terapeutska razblaženja. Potentnost Dpt vakcina praćena ELISA-inhibicijom u 4 terapeutska razblaženja, nakon 12 meseci zadržan je u svim razblaženjima u opsegu 65-80%. Ispitivanje je pokazalo da glicerolom stabilizovane Dpt vakcine za subligvalnu imunoterapiju, uz čuvanje na 4°C zadržavaju alergeni potencijal ( gt 65%) nakon 12 meseci od njihove pripreme, i kao takve mogu se koristiti za tretman alergije na kućne grinje.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Stability evaluation of house dust mite vaccines for sublingual immunotherapy, Ispitivanje stabilnosti vakcine kućne prašine za sublingvalnu imunoterapiju",
volume = "75",
number = "1",
pages = "19-26",
doi = "10.2298/JSC1001019B"
}

Burazer, L. M., Milovanovic, K., Ćirković-Veličković, T.,& Gavrović-Jankulović, M.. (2010). Stability evaluation of house dust mite vaccines for sublingual immunotherapy. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 75(1), 19-26.
https://doi.org/10.2298/JSC1001019B

Burazer LM, Milovanovic K, Ćirković-Veličković T, Gavrović-Jankulović M. Stability evaluation of house dust mite vaccines for sublingual immunotherapy. in Journal of the Serbian Chemical Society. 2010;75(1):19-26.
doi:10.2298/JSC1001019B .

Burazer, Lidija M., Milovanovic, Katarina, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, "Stability evaluation of house dust mite vaccines for sublingual immunotherapy" in Journal of the Serbian Chemical Society, 75, no. 1 (2010):19-26,
https://doi.org/10.2298/JSC1001019B . .

TY  - JOUR
AU  - Alexandru, Maria-Gabriela
AU  - Ćirković-Veličković, Tanja
AU  - Jitaru, Ioana
AU  - Grgurić-Šipka, Sanja
AU  - Draghici, Constantin
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1075
AB  - This paper presents the synthesis of complex compounds of type [M(L1)(2)], where M(II) = Cu (1), Co (2), Zn (3), L1 = 2-aminothiazole-4-acetate and [Mn(L1)(2)(H2O)] (4) using ethyl 2-(2-aminothiazole-4-yl) acetate (L), and characterization by elemental analysis, magnetic susceptibilities, IR, 1H-NMR, UV-Vis spectroscopy and for [Mn(L1)(2)(H2O)] also by X-ray diffraction. In vitro cytotoxicity studies were performed on human cervix adenocarcinoma, HeLa cells. The antitumor selectivity was assessed using normal human peripheral blood mononuclear cells, PBMC as control.
PB  - De Gruyter Poland Sp Zoo, Warsaw
T2  - Central European Journal of Chemistry
T1  - Synthesis, characterization and antitumor activity of Cu(II), Co(II), Zn(II) and Mn(II) complex compounds with aminothiazole acetate derivative
VL  - 8
IS  - 3
SP  - 639
EP  - 645
DO  - 10.2478/s11532-010-0022-2
ER  - 

@article{
author = "Alexandru, Maria-Gabriela and Ćirković-Veličković, Tanja and Jitaru, Ioana and Grgurić-Šipka, Sanja and Draghici, Constantin",
year = "2010",
abstract = "This paper presents the synthesis of complex compounds of type [M(L1)(2)], where M(II) = Cu (1), Co (2), Zn (3), L1 = 2-aminothiazole-4-acetate and [Mn(L1)(2)(H2O)] (4) using ethyl 2-(2-aminothiazole-4-yl) acetate (L), and characterization by elemental analysis, magnetic susceptibilities, IR, 1H-NMR, UV-Vis spectroscopy and for [Mn(L1)(2)(H2O)] also by X-ray diffraction. In vitro cytotoxicity studies were performed on human cervix adenocarcinoma, HeLa cells. The antitumor selectivity was assessed using normal human peripheral blood mononuclear cells, PBMC as control.",
publisher = "De Gruyter Poland Sp Zoo, Warsaw",
journal = "Central European Journal of Chemistry",
title = "Synthesis, characterization and antitumor activity of Cu(II), Co(II), Zn(II) and Mn(II) complex compounds with aminothiazole acetate derivative",
volume = "8",
number = "3",
pages = "639-645",
doi = "10.2478/s11532-010-0022-2"
}

Alexandru, M., Ćirković-Veličković, T., Jitaru, I., Grgurić-Šipka, S.,& Draghici, C.. (2010). Synthesis, characterization and antitumor activity of Cu(II), Co(II), Zn(II) and Mn(II) complex compounds with aminothiazole acetate derivative. in Central European Journal of Chemistry
De Gruyter Poland Sp Zoo, Warsaw., 8(3), 639-645.
https://doi.org/10.2478/s11532-010-0022-2

Alexandru M, Ćirković-Veličković T, Jitaru I, Grgurić-Šipka S, Draghici C. Synthesis, characterization and antitumor activity of Cu(II), Co(II), Zn(II) and Mn(II) complex compounds with aminothiazole acetate derivative. in Central European Journal of Chemistry. 2010;8(3):639-645.
doi:10.2478/s11532-010-0022-2 .

Alexandru, Maria-Gabriela, Ćirković-Veličković, Tanja, Jitaru, Ioana, Grgurić-Šipka, Sanja, Draghici, Constantin, "Synthesis, characterization and antitumor activity of Cu(II), Co(II), Zn(II) and Mn(II) complex compounds with aminothiazole acetate derivative" in Central European Journal of Chemistry, 8, no. 3 (2010):639-645,
https://doi.org/10.2478/s11532-010-0022-2 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Zivanovic, Mirjana
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Đurić, Vojislav
AU  - Sankovic-Babic, Snezana
AU  - Nestorovic, Branimir
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1111
AB  - Introduction Ingestion is the principal route for food allergens to trigger allergic reaction in atopic persons. However, in some highly sensitive patients severe symptoms may develop upon skin contact and by inhalation. The clinical spectrum ranges from mild facial urticaria and angioedema to life-threatening anaphylactic reactions. Outline of Cases We describe cases of severe anaphylactic reactions by skin contact, induced by kissing in five children with prior history of severe anaphylaxis caused by food ingestion. These cases were found to have the medical history of IgE mediated food allergy, a very high total and specific serum IgE level and very strong family history of allergy. Conclusion The presence of tiny particles of food on the kisser's lips was sufficient to trigger an anaphylactic reaction in sensitized children with prior history of severe allergic reaction caused by ingestion of food. Allergic reaction provoked with food allergens by skin contact can be a risk factor for generalized reactions. Therefore, extreme care has to be taken in avoiding kissing allergic children after eating foods to which they are highly allergic. Considering that kissing can be a cause of severe danger for the food allergic patient, such persons should inform their partners about the risk factor for causing their food hypersensitivity.
AB  - Uvod. Ingestija (unošenje hrane, tečnosti, lekova u telo kroz usta) je najčešći način nastanka alergije na hranu. Kod veoma osetljivih osoba, kod kojih je zastupljen visok nivo specifičnih IgE antitela u krvotoku na uzročnik alergije, sistemske reakcije mogu da se jave nakon kontakta s vrlo malim količinama alergena iz hrane putem kože ili udisanjem. Klinički simptomi variraju od pojave blage urtikarije na licu i angioedema do sistemske anafilaktičke reakcije. Prikaz bolesnika. Prikazani su slučajevi anafilaktične reakcije nastale nakon poljupca, tj. kontakta putem kože, kod petoro dece koja su imala već dokazanu alergiju na hranu. Kod sve dece su postojale jasna anamneza i klinička slika nutritivne alergije posredovane IgE, povišene vrednosti ukupnog i specifičnog IgE i pozitivna porodična anamneza u vezi s alergijama. Veoma male količine alergena na usnama bile su okidač za pokretanje sistemske anafilaktičke reakcije pri kontaktu s osobama kod kojih je već postojala reakcija na alergene iz hrane. Zaključak. Navedeni prikazi nedvosmisleno ukazuju na to da je neophodan dodatni oprez u ishrani dece sa dokazanom nutritivnom alergijom. Roditelji i ljudi iz okoline ove dece morali bi da vode računa o tome šta su pojeli pre nego što ih poljube, što važi i za adolescente s ovom alergijom. Takođe bi ih trebalo obavestiti o uzročnicima alergijske reakcije i na njene moguće posledice.
PB  - Srpsko Lekarsko Drustvo, Beograd
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Kiss-Induced Severe Anaphylactic Reactions
T1  - Anafilaktička reakcija izazvana poljupcem
VL  - 138
IS  - 7-8
SP  - 498
EP  - 501
DO  - 10.2298/SARH1008498A
ER  - 

@article{
author = "Atanasković-Marković, Marina and Zivanovic, Mirjana and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Đurić, Vojislav and Sankovic-Babic, Snezana and Nestorovic, Branimir",
year = "2010",
abstract = "Introduction Ingestion is the principal route for food allergens to trigger allergic reaction in atopic persons. However, in some highly sensitive patients severe symptoms may develop upon skin contact and by inhalation. The clinical spectrum ranges from mild facial urticaria and angioedema to life-threatening anaphylactic reactions. Outline of Cases We describe cases of severe anaphylactic reactions by skin contact, induced by kissing in five children with prior history of severe anaphylaxis caused by food ingestion. These cases were found to have the medical history of IgE mediated food allergy, a very high total and specific serum IgE level and very strong family history of allergy. Conclusion The presence of tiny particles of food on the kisser's lips was sufficient to trigger an anaphylactic reaction in sensitized children with prior history of severe allergic reaction caused by ingestion of food. Allergic reaction provoked with food allergens by skin contact can be a risk factor for generalized reactions. Therefore, extreme care has to be taken in avoiding kissing allergic children after eating foods to which they are highly allergic. Considering that kissing can be a cause of severe danger for the food allergic patient, such persons should inform their partners about the risk factor for causing their food hypersensitivity., Uvod. Ingestija (unošenje hrane, tečnosti, lekova u telo kroz usta) je najčešći način nastanka alergije na hranu. Kod veoma osetljivih osoba, kod kojih je zastupljen visok nivo specifičnih IgE antitela u krvotoku na uzročnik alergije, sistemske reakcije mogu da se jave nakon kontakta s vrlo malim količinama alergena iz hrane putem kože ili udisanjem. Klinički simptomi variraju od pojave blage urtikarije na licu i angioedema do sistemske anafilaktičke reakcije. Prikaz bolesnika. Prikazani su slučajevi anafilaktične reakcije nastale nakon poljupca, tj. kontakta putem kože, kod petoro dece koja su imala već dokazanu alergiju na hranu. Kod sve dece su postojale jasna anamneza i klinička slika nutritivne alergije posredovane IgE, povišene vrednosti ukupnog i specifičnog IgE i pozitivna porodična anamneza u vezi s alergijama. Veoma male količine alergena na usnama bile su okidač za pokretanje sistemske anafilaktičke reakcije pri kontaktu s osobama kod kojih je već postojala reakcija na alergene iz hrane. Zaključak. Navedeni prikazi nedvosmisleno ukazuju na to da je neophodan dodatni oprez u ishrani dece sa dokazanom nutritivnom alergijom. Roditelji i ljudi iz okoline ove dece morali bi da vode računa o tome šta su pojeli pre nego što ih poljube, što važi i za adolescente s ovom alergijom. Takođe bi ih trebalo obavestiti o uzročnicima alergijske reakcije i na njene moguće posledice.",
publisher = "Srpsko Lekarsko Drustvo, Beograd",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Kiss-Induced Severe Anaphylactic Reactions, Anafilaktička reakcija izazvana poljupcem",
volume = "138",
number = "7-8",
pages = "498-501",
doi = "10.2298/SARH1008498A"
}

Atanasković-Marković, M., Zivanovic, M., Gavrović-Jankulović, M., Ćirković-Veličković, T., Đurić, V., Sankovic-Babic, S.,& Nestorovic, B.. (2010). Kiss-Induced Severe Anaphylactic Reactions. in Srpski arhiv za celokupno lekarstvo
Srpsko Lekarsko Drustvo, Beograd., 138(7-8), 498-501.
https://doi.org/10.2298/SARH1008498A

Atanasković-Marković M, Zivanovic M, Gavrović-Jankulović M, Ćirković-Veličković T, Đurić V, Sankovic-Babic S, Nestorovic B. Kiss-Induced Severe Anaphylactic Reactions. in Srpski arhiv za celokupno lekarstvo. 2010;138(7-8):498-501.
doi:10.2298/SARH1008498A .

Atanasković-Marković, Marina, Zivanovic, Mirjana, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Đurić, Vojislav, Sankovic-Babic, Snezana, Nestorovic, Branimir, "Kiss-Induced Severe Anaphylactic Reactions" in Srpski arhiv za celokupno lekarstvo, 138, no. 7-8 (2010):498-501,
https://doi.org/10.2298/SARH1008498A . .

TY  - JOUR
AU  - Perovic, I.
AU  - Milovanovic, M.
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/600
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
VL  - 39
IS  - 3
SP  - 435
EP  - 446
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perovic, I. and Milovanovic, M. and Stanić, Dragana and Burazer, Lidija M. and Petrović, D. and Milčić-Matić, Natalija and Gafvelin, Guro and van Hage, Marianne and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
volume = "39",
number = "3",
pages = "435-446",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perovic, I., Milovanovic, M., Stanić, D., Burazer, L. M., Petrović, D., Milčić-Matić, N., Gafvelin, G., van Hage, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perovic I, Milovanovic M, Stanić D, Burazer LM, Petrović D, Milčić-Matić N, Gafvelin G, van Hage M, Jankov RM, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perovic, I., Milovanovic, M., Stanić, Dragana, Burazer, Lidija M., Petrović, D., Milčić-Matić, Natalija, Gafvelin, Guro, van Hage, Marianne, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

TY  - JOUR
AU  - Aćimović, Jelena M.
AU  - Stanimirović, Bojana
AU  - Mandić, Ljuba M.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1015
AB  - Methylglyoxal is a highly reactive a-oxoaldehyde with elevated production in hyperglycemia. It reacts with nucleophilic Lys and Arg side-chains and N-terminal amino groups causing protein modification. In the present study, the importance of the reaction of the Cys thiol group with methylglyoxal in protein modification, the competitiveness of this reaction with those of amino and guanidine groups, the time course of these reactions and their role and contribution to protein cross-linking were investigated. Human and bovine serum albumins were used as model systems. It was found that despite the very low levels of thiol groups on the surface of the examined protein molecules (approx. 80 times lower than those of amino and guanidino groups), a very high percentage of it reacts (25-85%). The amount of reacted thiol groups and the rate of the reaction, the time for the reaction to reach equilibrium, the formation of a stable product and the contribution of thiol groups to protein cross-linking depend on the methylglyoxal concentration. The product formed in the reaction of thiol and an insufficient quantity of methylglyoxal (compared to the concentrations of the groups accessible for modification) participates to a significant extent (4%) to protein cross-linking. Metformin applied in equimolar concentration with methylglyoxal prevents its reaction with amino and guanidino groups but, however, not with thiol groups.
AB  - Metilglioksal je veoma reaktivni α-oksoaldehid koji se povećano stvara u hiperglikemiji. Reaguje sa nukleofilnim grupama bočnih ostataka Lys, Arg i N-terminalnom amino-grupom, što dovodi do modifikacije proteina. U ovom radu ispitivani su značaj reakcije SH grupe sa metilglioksalom u modifikaciji proteina, konkurentnost ove reakcije u odnosu na reakcije sa amino- i gvanidino-grupom, tok ovih reakcija i njihova uloga i doprinos u umrežavanju proteina. Kao model-sistemi upotrebljeni su humani i goveđi serum-albumin. Utvrđeno je da i pored veoma male zastupljenosti SH grupe na površini ispitivanih molekula proteina (oko 80 puta manja u odnosu na ukupan broj amino- i gvanidino-grupa), ona reaguje u velikom procentu (od 25-85 %). Količina izreagovanih SH grupa i brzina reakcije, vreme uspostavljanja ravnoteže reakcije, stvaranja stabilnog proizvoda i doprinos SH grupa umrežavanju proteina zavise od koncentracije metilglioksala. Proizvod stvoren u reakciji SH grupa i nedovoljne količine metilglioksala (u odnosu na koncentraciju grupa dostupnih za modifikaciju) učestvuje u umrežavanju proteina sa značajnim udelom (4 %). U ekvimolarnoj koncentraciji sa metilglioksalom metformin sprečava njegovu reakciju sa amino i guanidino grupama albumina, ali ne i sa tiol grupom.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - The role of the thiol group in protein modification with methylglyoxal
T1  - Uloga tiolne grupe u modifikaciji proteina sa metilglioksalom
VL  - 74
IS  - 8-9
SP  - 867
EP  - 883
DO  - 10.2298/JSC0909867A
ER  - 

@article{
author = "Aćimović, Jelena M. and Stanimirović, Bojana and Mandić, Ljuba M.",
year = "2009",
abstract = "Methylglyoxal is a highly reactive a-oxoaldehyde with elevated production in hyperglycemia. It reacts with nucleophilic Lys and Arg side-chains and N-terminal amino groups causing protein modification. In the present study, the importance of the reaction of the Cys thiol group with methylglyoxal in protein modification, the competitiveness of this reaction with those of amino and guanidine groups, the time course of these reactions and their role and contribution to protein cross-linking were investigated. Human and bovine serum albumins were used as model systems. It was found that despite the very low levels of thiol groups on the surface of the examined protein molecules (approx. 80 times lower than those of amino and guanidino groups), a very high percentage of it reacts (25-85%). The amount of reacted thiol groups and the rate of the reaction, the time for the reaction to reach equilibrium, the formation of a stable product and the contribution of thiol groups to protein cross-linking depend on the methylglyoxal concentration. The product formed in the reaction of thiol and an insufficient quantity of methylglyoxal (compared to the concentrations of the groups accessible for modification) participates to a significant extent (4%) to protein cross-linking. Metformin applied in equimolar concentration with methylglyoxal prevents its reaction with amino and guanidino groups but, however, not with thiol groups., Metilglioksal je veoma reaktivni α-oksoaldehid koji se povećano stvara u hiperglikemiji. Reaguje sa nukleofilnim grupama bočnih ostataka Lys, Arg i N-terminalnom amino-grupom, što dovodi do modifikacije proteina. U ovom radu ispitivani su značaj reakcije SH grupe sa metilglioksalom u modifikaciji proteina, konkurentnost ove reakcije u odnosu na reakcije sa amino- i gvanidino-grupom, tok ovih reakcija i njihova uloga i doprinos u umrežavanju proteina. Kao model-sistemi upotrebljeni su humani i goveđi serum-albumin. Utvrđeno je da i pored veoma male zastupljenosti SH grupe na površini ispitivanih molekula proteina (oko 80 puta manja u odnosu na ukupan broj amino- i gvanidino-grupa), ona reaguje u velikom procentu (od 25-85 %). Količina izreagovanih SH grupa i brzina reakcije, vreme uspostavljanja ravnoteže reakcije, stvaranja stabilnog proizvoda i doprinos SH grupa umrežavanju proteina zavise od koncentracije metilglioksala. Proizvod stvoren u reakciji SH grupa i nedovoljne količine metilglioksala (u odnosu na koncentraciju grupa dostupnih za modifikaciju) učestvuje u umrežavanju proteina sa značajnim udelom (4 %). U ekvimolarnoj koncentraciji sa metilglioksalom metformin sprečava njegovu reakciju sa amino i guanidino grupama albumina, ali ne i sa tiol grupom.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "The role of the thiol group in protein modification with methylglyoxal, Uloga tiolne grupe u modifikaciji proteina sa metilglioksalom",
volume = "74",
number = "8-9",
pages = "867-883",
doi = "10.2298/JSC0909867A"
}

Aćimović, J. M., Stanimirović, B.,& Mandić, L. M.. (2009). The role of the thiol group in protein modification with methylglyoxal. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 74(8-9), 867-883.
https://doi.org/10.2298/JSC0909867A

Aćimović JM, Stanimirović B, Mandić LM. The role of the thiol group in protein modification with methylglyoxal. in Journal of the Serbian Chemical Society. 2009;74(8-9):867-883.
doi:10.2298/JSC0909867A .

Aćimović, Jelena M., Stanimirović, Bojana, Mandić, Ljuba M., "The role of the thiol group in protein modification with methylglyoxal" in Journal of the Serbian Chemical Society, 74, no. 8-9 (2009):867-883,
https://doi.org/10.2298/JSC0909867A . .

TY  - JOUR
AU  - Dimitrijevic, R.
AU  - Stojanovic, M.
AU  - Živković, Irena
AU  - Petersen, A.
AU  - Jankov, Ratko M.
AU  - Dimitrijevic, L.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1028
AB  - Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
VL  - 107
IS  - 6
SP  - 2108
EP  - 2115
DO  - 10.1111/j.1365-2672.2009.04539.x
ER  - 

@article{
author = "Dimitrijevic, R. and Stojanovic, M. and Živković, Irena and Petersen, A. and Jankov, Ratko M. and Dimitrijevic, L. and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
volume = "107",
number = "6",
pages = "2108-2115",
doi = "10.1111/j.1365-2672.2009.04539.x"
}

Dimitrijevic, R., Stojanovic, M., Živković, I., Petersen, A., Jankov, R. M., Dimitrijevic, L.,& Gavrović-Jankulović, M.. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology
Wiley-Blackwell, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x

Dimitrijevic R, Stojanovic M, Živković I, Petersen A, Jankov RM, Dimitrijevic L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology. 2009;107(6):2108-2115.
doi:10.1111/j.1365-2672.2009.04539.x .

Dimitrijevic, R., Stojanovic, M., Živković, Irena, Petersen, A., Jankov, Ratko M., Dimitrijevic, L., Gavrović-Jankulović, Marija, "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68" in Journal of Applied Microbiology, 107, no. 6 (2009):2108-2115,
https://doi.org/10.1111/j.1365-2672.2009.04539.x . .

TY  - JOUR
AU  - Milovanovic, Katarina
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/992
AB  - House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment.
AB  - Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus
T1  - Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja
VL  - 74
IS  - 5
SP  - 513
EP  - 522
DO  - 10.2298/JSC0905513M
ER  - 

@article{
author = "Milovanovic, Katarina and Burazer, Lidija M. and Vučković, Olga and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment., Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus, Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja",
volume = "74",
number = "5",
pages = "513-522",
doi = "10.2298/JSC0905513M"
}

Milovanovic, K., Burazer, L. M., Vučković, O., Atanasković-Marković, M., Ćirković-Veličković, T., Jankov, R. M.,& Gavrović-Jankulović, M.. (2009). Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 74(5), 513-522.
https://doi.org/10.2298/JSC0905513M

Milovanovic K, Burazer LM, Vučković O, Atanasković-Marković M, Ćirković-Veličković T, Jankov RM, Gavrović-Jankulović M. Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society. 2009;74(5):513-522.
doi:10.2298/JSC0905513M .

Milovanovic, Katarina, Burazer, Lidija M., Vučković, Olga, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, Jankov, Ratko M., Gavrović-Jankulović, Marija, "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus" in Journal of the Serbian Chemical Society, 74, no. 5 (2009):513-522,
https://doi.org/10.2298/JSC0905513M . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Radosavljević, Jelena
AU  - Polović, Natalija
AU  - Jadranin, Milka
AU  - Popović, Milica
AU  - Vučković, Olga
AU  - Burazer, Lidija M.
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1019
AB  - The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on beta-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Dairy Journal
T1  - Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation
VL  - 19
IS  - 12
SP  - 746
EP  - 752
DO  - 10.1016/j.idairyj.2009.05.008
ER  - 

@article{
author = "Stanić, Dragana and Radosavljević, Jelena and Polović, Natalija and Jadranin, Milka and Popović, Milica and Vučković, Olga and Burazer, Lidija M. and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "The use of enzymes may improve the functional properties of various food ingredients. The aim of this study was to examine the effects of proteolytic contaminants in phenol oxidases on beta-lactoglobulin (BLG). In the presence of Trametes versicolor laccase and Agaricus bisporus tyrosinase, both variants of BLG (A and B) underwent removal of a peptide from the N-terminus. The truncated forms were more susceptible to digestion by pepsin. The truncation of BLG resulted from contaminating proteases and not due to the action of phenol oxidases. The removal of N-terminal peptides proceeded quickly, while the rest of the globular protein remained resistant to proteolysis for up to 3 h. In the case of the application of enzymes in food bioprocessing, it may be important to carefully monitor the effects of contaminating proteases in enzyme preparations used. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Dairy Journal",
title = "Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation",
volume = "19",
number = "12",
pages = "746-752",
doi = "10.1016/j.idairyj.2009.05.008"
}

Stanić, D., Radosavljević, J., Polović, N., Jadranin, M., Popović, M., Vučković, O., Burazer, L. M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal
Elsevier Sci Ltd, Oxford., 19(12), 746-752.
https://doi.org/10.1016/j.idairyj.2009.05.008

Stanić D, Radosavljević J, Polović N, Jadranin M, Popović M, Vučković O, Burazer LM, Jankov RM, Ćirković-Veličković T. Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation. in International Dairy Journal. 2009;19(12):746-752.
doi:10.1016/j.idairyj.2009.05.008 .

Stanić, Dragana, Radosavljević, Jelena, Polović, Natalija, Jadranin, Milka, Popović, Milica, Vučković, Olga, Burazer, Lidija M., Jankov, Ratko M., Ćirković-Veličković, Tanja, "Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation" in International Dairy Journal, 19, no. 12 (2009):746-752,
https://doi.org/10.1016/j.idairyj.2009.05.008 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Pjanovic, Rada V.
AU  - Burazer, Lidija M.
AU  - Veličković, Sava
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/592
AB  - BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system. (C) 2008 Society of Chemical Industry
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion
VL  - 89
IS  - 1
SP  - 8
EP  - 14
DO  - 10.1002/jsfa.3404
ER  - 

@article{
author = "Polović, Natalija and Pjanovic, Rada V. and Burazer, Lidija M. and Veličković, Sava and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system. (C) 2008 Society of Chemical Industry",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion",
volume = "89",
number = "1",
pages = "8-14",
doi = "10.1002/jsfa.3404"
}

Polović, N., Pjanovic, R. V., Burazer, L. M., Veličković, S., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 89(1), 8-14.
https://doi.org/10.1002/jsfa.3404

Polović N, Pjanovic RV, Burazer LM, Veličković S, Jankov RM, Ćirković-Veličković T. Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture. 2009;89(1):8-14.
doi:10.1002/jsfa.3404 .

Polović, Natalija, Pjanovic, Rada V., Burazer, Lidija M., Veličković, Sava, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion" in Journal of the Science of Food and Agriculture, 89, no. 1 (2009):8-14,
https://doi.org/10.1002/jsfa.3404 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/988
AB  - Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids.
AB  - Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation
T1  - Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem
VL  - 74
IS  - 4
SP  - 359
EP  - 366
DO  - 10.2298/JSC0904359S
ER  - 

@article{
author = "Stanić, Dragana and Burazer, Lidija M. and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v I that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified ammo groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids., Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation, Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem",
volume = "74",
number = "4",
pages = "359-366",
doi = "10.2298/JSC0904359S"
}

Stanić, D., Burazer, L. M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 74(4), 359-366.
https://doi.org/10.2298/JSC0904359S

Stanić D, Burazer LM, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society. 2009;74(4):359-366.
doi:10.2298/JSC0904359S .

Stanić, Dragana, Burazer, Lidija M., Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation" in Journal of the Serbian Chemical Society, 74, no. 4 (2009):359-366,
https://doi.org/10.2298/JSC0904359S . .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Spasic, Milena
AU  - Ćirković-Veličković, Tanja
AU  - Stojanović, Marijana M.
AU  - Inić-Kanada, Aleksandra
AU  - Dimitrijevic, Ljiliana
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Becker, Wolf-Meinhard
AU  - Jankov, Ratko M.
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/948
AB  - Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwi fruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.
PB  - Wiley-Blackwell, Malden
T2  - Molecular Nutrition and Food Research
T1  - Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA
VL  - 52
IS  - 6
SP  - 701
EP  - 707
DO  - 10.1002/mnfr.200700286
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Spasic, Milena and Ćirković-Veličković, Tanja and Stojanović, Marijana M. and Inić-Kanada, Aleksandra and Dimitrijevic, Ljiliana and Lindner, Buko and Petersen, Arnd and Becker, Wolf-Meinhard and Jankov, Ratko M.",
year = "2008",
abstract = "Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwi fruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.",
publisher = "Wiley-Blackwell, Malden",
journal = "Molecular Nutrition and Food Research",
title = "Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA",
volume = "52",
number = "6",
pages = "701-707",
doi = "10.1002/mnfr.200700286"
}

Gavrović-Jankulović, M., Spasic, M., Ćirković-Veličković, T., Stojanović, M. M., Inić-Kanada, A., Dimitrijevic, L., Lindner, B., Petersen, A., Becker, W.,& Jankov, R. M.. (2008). Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA. in Molecular Nutrition and Food Research
Wiley-Blackwell, Malden., 52(6), 701-707.
https://doi.org/10.1002/mnfr.200700286

Gavrović-Jankulović M, Spasic M, Ćirković-Veličković T, Stojanović MM, Inić-Kanada A, Dimitrijevic L, Lindner B, Petersen A, Becker W, Jankov RM. Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA. in Molecular Nutrition and Food Research. 2008;52(6):701-707.
doi:10.1002/mnfr.200700286 .

Gavrović-Jankulović, Marija, Spasic, Milena, Ćirković-Veličković, Tanja, Stojanović, Marijana M., Inić-Kanada, Aleksandra, Dimitrijevic, Ljiliana, Lindner, Buko, Petersen, Arnd, Becker, Wolf-Meinhard, Jankov, Ratko M., "Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA" in Molecular Nutrition and Food Research, 52, no. 6 (2008):701-707,
https://doi.org/10.1002/mnfr.200700286 . .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Poulsen, Knud
AU  - Brckalo, Tamara
AU  - Bobic, Sonja
AU  - Lindner, Buko
AU  - Petersen, Arnd
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/929
AB  - Lectins as carbohydrate-binding proteins have been employed in various biological assays for the detection and characterization of glycan structures on glycoproteins, including clinical biomarkers in disease states. A mannose-specific banana lectin (BanLec) is unique in its specificity for internal alpha 1,3 linkages as well as beta 1,3 linkages at the reducing termini. The immunomodulatory potential of natural BanLec was recognized by a strong immunoglobulin G4 antibody response and T cell mitogen activity in humans. To explore its applicability in glycoproteomics and its modulatory potential, the gene of banana lectin was cloned, sequenced and a recombinant protein was produced in Escherichia coli. The obtained cDNA revealed a novel banana lectin isoform, with an open reading frame of 426 nucleotides, encoding a cytoplasmatic protein of 141 amino acids. The molecular mass of rBanLec determined by ESI FT-MS and N-terminal sequencing confirmed the cDNA at the protein level. The specificity of rBanLec for detection glycan structures was the same as for natural BanLec, as examined with five protein extracts rich in glycoprotein content, as well as with horseradish peroxidase glycoprotein. Besides, the immunomodulatory potential of rBanLec and nBanLec were comparable as assessed by an inhibition assay and a human T cell proliferation assay where they induced a strong proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs. This recombinant BanLec is a useful reagent for glycoprotcomics and lectin microarrays, with a potential for modulation of the immune response. (C) 2007 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - International Journal of Biochemistry and Cell Biology
T1  - A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs
VL  - 40
IS  - 5
SP  - 929
EP  - 941
DO  - 10.1016/j.biocel.2007.10.033
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Poulsen, Knud and Brckalo, Tamara and Bobic, Sonja and Lindner, Buko and Petersen, Arnd",
year = "2008",
abstract = "Lectins as carbohydrate-binding proteins have been employed in various biological assays for the detection and characterization of glycan structures on glycoproteins, including clinical biomarkers in disease states. A mannose-specific banana lectin (BanLec) is unique in its specificity for internal alpha 1,3 linkages as well as beta 1,3 linkages at the reducing termini. The immunomodulatory potential of natural BanLec was recognized by a strong immunoglobulin G4 antibody response and T cell mitogen activity in humans. To explore its applicability in glycoproteomics and its modulatory potential, the gene of banana lectin was cloned, sequenced and a recombinant protein was produced in Escherichia coli. The obtained cDNA revealed a novel banana lectin isoform, with an open reading frame of 426 nucleotides, encoding a cytoplasmatic protein of 141 amino acids. The molecular mass of rBanLec determined by ESI FT-MS and N-terminal sequencing confirmed the cDNA at the protein level. The specificity of rBanLec for detection glycan structures was the same as for natural BanLec, as examined with five protein extracts rich in glycoprotein content, as well as with horseradish peroxidase glycoprotein. Besides, the immunomodulatory potential of rBanLec and nBanLec were comparable as assessed by an inhibition assay and a human T cell proliferation assay where they induced a strong proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs. This recombinant BanLec is a useful reagent for glycoprotcomics and lectin microarrays, with a potential for modulation of the immune response. (C) 2007 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "International Journal of Biochemistry and Cell Biology",
title = "A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs",
volume = "40",
number = "5",
pages = "929-941",
doi = "10.1016/j.biocel.2007.10.033"
}

Gavrović-Jankulović, M., Poulsen, K., Brckalo, T., Bobic, S., Lindner, B.,& Petersen, A.. (2008). A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs. in International Journal of Biochemistry and Cell Biology
Pergamon-Elsevier Science Ltd, Oxford., 40(5), 929-941.
https://doi.org/10.1016/j.biocel.2007.10.033

Gavrović-Jankulović M, Poulsen K, Brckalo T, Bobic S, Lindner B, Petersen A. A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs. in International Journal of Biochemistry and Cell Biology. 2008;40(5):929-941.
doi:10.1016/j.biocel.2007.10.033 .

Gavrović-Jankulović, Marija, Poulsen, Knud, Brckalo, Tamara, Bobic, Sonja, Lindner, Buko, Petersen, Arnd, "A novel recombinantly produced banana lectin isoform is a valuable tool for glycoproteomics and a potent modulator of the proliferation response in CD3(+), CD4(+), and CD8(+) populations of human PBMCs" in International Journal of Biochemistry and Cell Biology, 40, no. 5 (2008):929-941,
https://doi.org/10.1016/j.biocel.2007.10.033 . .

TY  - JOUR
AU  - Jovanović, Vesna B.
AU  - Dimitrijevic-Sreckovic, V. S.
AU  - Mandić, Ljuba M.
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/958
AB  - The connection between changes in the activity of serum N-acetyl-beta-D-glucosaminidase (NAG, E.C.3.2.1.30) and iso-enzymes and degree of secondary complications was analyzed in four groups of type 1 diabetic patients (n=69): without complications (n=22); with retinopathy (n=16); with retinopathy and polyneuropathy (n= 13), and with retinopathy, neuropathy, and nephropathy (n=18). In all groups statistically significant higher (P  lt  0.001) percent fraction of A form (83.84 +/- 6.09, 84.37 +/- 5.74, 81.76 +/- 6.02, 76.37 +/- 7.38%, resp.) and lower (P  lt  0.001, P  lt  0.01) fraction of B form (15.87 +/- 5.65, 15.66 +/- 5.74, 18.33 +/- 5.98, 23.63 +/- 7.38, resp.) in total NAG compared with the control (A = 69.38 +/- 4.79%, B = 30.61 +/- 4.78%) were found. The differences in A as well as B forms between diabetic groups were not statistically significant. Significant strong positive correlations between total NAG and glycemia (0.494-0.623), total NAG and A form (0.934-0.966), and A form and glycemia (0.512-0.638) were found in all groups. No correlation was found between the fractions of B and A forms, except in the fourth group. The A form of diabetic patients in the fourth group was more acidic compared with the control and other diabetic groups. It was concluded that the changes in serum NAG and isoenzymic profiles in diabetes are the consequence of its increased exocytose, especially of the A form, in hyperglycemia and posttranslational modifications of iso-enzymes. The total activity of serum NAG and iso-enzymic profiles cannot be used for monitoring the development and distinction of type 1 diabetes secondary complications.
PB  - Wiley-Liss, Hoboken
T2  - Journal of Clinical Laboratory Analysis
T1  - Serum N-acetyl-beta-D-glucosaminidase profiles in type 1 diabetes secondary complications: Causes of changes and significance of determination
VL  - 22
IS  - 4
SP  - 307
EP  - 313
DO  - 10.1002/jcla.20262
ER  - 

@article{
author = "Jovanović, Vesna B. and Dimitrijevic-Sreckovic, V. S. and Mandić, Ljuba M.",
year = "2008",
abstract = "The connection between changes in the activity of serum N-acetyl-beta-D-glucosaminidase (NAG, E.C.3.2.1.30) and iso-enzymes and degree of secondary complications was analyzed in four groups of type 1 diabetic patients (n=69): without complications (n=22); with retinopathy (n=16); with retinopathy and polyneuropathy (n= 13), and with retinopathy, neuropathy, and nephropathy (n=18). In all groups statistically significant higher (P  lt  0.001) percent fraction of A form (83.84 +/- 6.09, 84.37 +/- 5.74, 81.76 +/- 6.02, 76.37 +/- 7.38%, resp.) and lower (P  lt  0.001, P  lt  0.01) fraction of B form (15.87 +/- 5.65, 15.66 +/- 5.74, 18.33 +/- 5.98, 23.63 +/- 7.38, resp.) in total NAG compared with the control (A = 69.38 +/- 4.79%, B = 30.61 +/- 4.78%) were found. The differences in A as well as B forms between diabetic groups were not statistically significant. Significant strong positive correlations between total NAG and glycemia (0.494-0.623), total NAG and A form (0.934-0.966), and A form and glycemia (0.512-0.638) were found in all groups. No correlation was found between the fractions of B and A forms, except in the fourth group. The A form of diabetic patients in the fourth group was more acidic compared with the control and other diabetic groups. It was concluded that the changes in serum NAG and isoenzymic profiles in diabetes are the consequence of its increased exocytose, especially of the A form, in hyperglycemia and posttranslational modifications of iso-enzymes. The total activity of serum NAG and iso-enzymic profiles cannot be used for monitoring the development and distinction of type 1 diabetes secondary complications.",
publisher = "Wiley-Liss, Hoboken",
journal = "Journal of Clinical Laboratory Analysis",
title = "Serum N-acetyl-beta-D-glucosaminidase profiles in type 1 diabetes secondary complications: Causes of changes and significance of determination",
volume = "22",
number = "4",
pages = "307-313",
doi = "10.1002/jcla.20262"
}

Jovanović, V. B., Dimitrijevic-Sreckovic, V. S.,& Mandić, L. M.. (2008). Serum N-acetyl-beta-D-glucosaminidase profiles in type 1 diabetes secondary complications: Causes of changes and significance of determination. in Journal of Clinical Laboratory Analysis
Wiley-Liss, Hoboken., 22(4), 307-313.
https://doi.org/10.1002/jcla.20262

Jovanović VB, Dimitrijevic-Sreckovic VS, Mandić LM. Serum N-acetyl-beta-D-glucosaminidase profiles in type 1 diabetes secondary complications: Causes of changes and significance of determination. in Journal of Clinical Laboratory Analysis. 2008;22(4):307-313.
doi:10.1002/jcla.20262 .

Jovanović, Vesna B., Dimitrijevic-Sreckovic, V. S., Mandić, Ljuba M., "Serum N-acetyl-beta-D-glucosaminidase profiles in type 1 diabetes secondary complications: Causes of changes and significance of determination" in Journal of Clinical Laboratory Analysis, 22, no. 4 (2008):307-313,
https://doi.org/10.1002/jcla.20262 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Vuckovic, Olja
AU  - Ivanovski, Petar
AU  - Nestorivic, Branimir
AU  - Cuturilo, Goran
AU  - Simic, Dusica
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/970
AB  - Natural rubber latex is the second most implicated agent in intraoperative anaphylactic reactions. This report describes a case of intraoperative anaphylaxis occurring in a non-atopic fourteen-year-old girl undergoing multiple surgical procedures, but without spina bifida, in which latex surgical gloves were the main culprit for the anaphylactic reactions. Clinical manifestations of an anaphylactic reaction were also experienced during the examination of the possible cause of intraoperative anaphylaxis by skin prick testing with a latex allergen extract. Skin tests with anesthetics were negative. Specific IgE to latex was positive at 92.9 kUA/L (class 5). The molecular basis for the reported intraoperative anaphylaxis was ascribed to three low-molecular mass latex allergens (10-15 kD) detected in the brand of latex surgical gloves used during the operation. Given the potential of a dramatic outcome, latex allergy, testing as a regular preoperative measure may contribute to the reduction of anaphylactic reactions during surgical interventions.
PB  - Tehran Univ Medical Sciences, Tehran
T2  - Iranian Journal of Allergy Asthma and Immunology
T1  - Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity
VL  - 7
IS  - 2
SP  - 97
EP  - 99
UR  - https://hdl.handle.net/21.15107/rcub_cherry_970
ER  - 

@article{
author = "Atanasković-Marković, Marina and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Vuckovic, Olja and Ivanovski, Petar and Nestorivic, Branimir and Cuturilo, Goran and Simic, Dusica",
year = "2008",
abstract = "Natural rubber latex is the second most implicated agent in intraoperative anaphylactic reactions. This report describes a case of intraoperative anaphylaxis occurring in a non-atopic fourteen-year-old girl undergoing multiple surgical procedures, but without spina bifida, in which latex surgical gloves were the main culprit for the anaphylactic reactions. Clinical manifestations of an anaphylactic reaction were also experienced during the examination of the possible cause of intraoperative anaphylaxis by skin prick testing with a latex allergen extract. Skin tests with anesthetics were negative. Specific IgE to latex was positive at 92.9 kUA/L (class 5). The molecular basis for the reported intraoperative anaphylaxis was ascribed to three low-molecular mass latex allergens (10-15 kD) detected in the brand of latex surgical gloves used during the operation. Given the potential of a dramatic outcome, latex allergy, testing as a regular preoperative measure may contribute to the reduction of anaphylactic reactions during surgical interventions.",
publisher = "Tehran Univ Medical Sciences, Tehran",
journal = "Iranian Journal of Allergy Asthma and Immunology",
title = "Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity",
volume = "7",
number = "2",
pages = "97-99",
url = "https://hdl.handle.net/21.15107/rcub_cherry_970"
}

Atanasković-Marković, M., Gavrović-Jankulović, M., Ćirković-Veličković, T., Vuckovic, O., Ivanovski, P., Nestorivic, B., Cuturilo, G.,& Simic, D.. (2008). Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity. in Iranian Journal of Allergy Asthma and Immunology
Tehran Univ Medical Sciences, Tehran., 7(2), 97-99.
https://hdl.handle.net/21.15107/rcub_cherry_970

Atanasković-Marković M, Gavrović-Jankulović M, Ćirković-Veličković T, Vuckovic O, Ivanovski P, Nestorivic B, Cuturilo G, Simic D. Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity. in Iranian Journal of Allergy Asthma and Immunology. 2008;7(2):97-99.
https://hdl.handle.net/21.15107/rcub_cherry_970 .

Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Vuckovic, Olja, Ivanovski, Petar, Nestorivic, Branimir, Cuturilo, Goran, Simic, Dusica, "Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity" in Iranian Journal of Allergy Asthma and Immunology, 7, no. 2 (2008):97-99,
https://hdl.handle.net/21.15107/rcub_cherry_970 .

TY  - JOUR
AU  - Blanusa, Milan
AU  - Perovic, Iva
AU  - Popović, Milica
AU  - Polović, Natalija
AU  - Burazer, Lidija M.
AU  - Milovanovic, Mina
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/885
AB  - A simple ion-exchange HPLC-UV method was developed for determination of major allergens from mugwort pollen and kiwi fruit extracts in mass-units. The separation of Art v 1 and Act c 1 from other components in the extracts was achieved in one step. The extinction coefficients used in the study here theoretically determined and compared to the extinction coefficients determined by gravimetry. We also reported a close correlation of the major allergen contents with the overall allergenic potency of the extracts determined by inhibition ELISA. This method could be a useful tool for standardization of allergenic extracts for clinical use. (c) 2007 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Chromatography B: Analytical Technologies in the Biomedical and L
T1  - Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method
VL  - 857
IS  - 2
SP  - 188
EP  - 194
DO  - 10.1016/j.jchromb.2007.07.015
ER  - 

@article{
author = "Blanusa, Milan and Perovic, Iva and Popović, Milica and Polović, Natalija and Burazer, Lidija M. and Milovanovic, Mina and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2007",
abstract = "A simple ion-exchange HPLC-UV method was developed for determination of major allergens from mugwort pollen and kiwi fruit extracts in mass-units. The separation of Art v 1 and Act c 1 from other components in the extracts was achieved in one step. The extinction coefficients used in the study here theoretically determined and compared to the extinction coefficients determined by gravimetry. We also reported a close correlation of the major allergen contents with the overall allergenic potency of the extracts determined by inhibition ELISA. This method could be a useful tool for standardization of allergenic extracts for clinical use. (c) 2007 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Chromatography B: Analytical Technologies in the Biomedical and L",
title = "Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method",
volume = "857",
number = "2",
pages = "188-194",
doi = "10.1016/j.jchromb.2007.07.015"
}

Blanusa, M., Perovic, I., Popović, M., Polović, N., Burazer, L. M., Milovanovic, M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2007). Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method. in Journal of Chromatography B: Analytical Technologies in the Biomedical and L
Elsevier Science Bv, Amsterdam., 857(2), 188-194.
https://doi.org/10.1016/j.jchromb.2007.07.015

Blanusa M, Perovic I, Popović M, Polović N, Burazer LM, Milovanovic M, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method. in Journal of Chromatography B: Analytical Technologies in the Biomedical and L. 2007;857(2):188-194.
doi:10.1016/j.jchromb.2007.07.015 .

Blanusa, Milan, Perovic, Iva, Popović, Milica, Polović, Natalija, Burazer, Lidija M., Milovanovic, Mina, Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method" in Journal of Chromatography B: Analytical Technologies in the Biomedical and L, 857, no. 2 (2007):188-194,
https://doi.org/10.1016/j.jchromb.2007.07.015 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Blanusa, M.
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/827
AB  - Background It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.
PB  - Blackwell Publishing, Oxford
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
VL  - 37
IS  - 5
SP  - 764
EP  - 771
DO  - 10.1111/j.1365-2222.2007.02703.x
ER  - 

@article{
author = "Polović, Natalija and Blanusa, M. and Gavrović-Jankulović, Marija and Atanasković-Marković, Marina and Burazer, Lidija M. and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2007",
abstract = "Background It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.",
publisher = "Blackwell Publishing, Oxford",
journal = "Clinical and Experimental Allergy",
title = "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro",
volume = "37",
number = "5",
pages = "764-771",
doi = "10.1111/j.1365-2222.2007.02703.x"
}

Polović, N., Blanusa, M., Gavrović-Jankulović, M., Atanasković-Marković, M., Burazer, L. M., Jankov, R. M.,& Ćirković-Veličković, T.. (2007). A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy
Blackwell Publishing, Oxford., 37(5), 764-771.
https://doi.org/10.1111/j.1365-2222.2007.02703.x

Polović N, Blanusa M, Gavrović-Jankulović M, Atanasković-Marković M, Burazer LM, Jankov RM, Ćirković-Veličković T. A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy. 2007;37(5):764-771.
doi:10.1111/j.1365-2222.2007.02703.x .

Polović, Natalija, Blanusa, M., Gavrović-Jankulović, Marija, Atanasković-Marković, Marina, Burazer, Lidija M., Jankov, Ratko M., Ćirković-Veličković, Tanja, "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro" in Clinical and Experimental Allergy, 37, no. 5 (2007):764-771,
https://doi.org/10.1111/j.1365-2222.2007.02703.x . .