Jankov, Ratko M.

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  • Jankov, Ratko M. (58)

Author's Bibliography

In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit

Popović, Milica; Bulajic, Aleksandra; Ristic, Danijela; Krstic, Branka; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Hoboken, 2012)

TY  - JOUR
AU  - Popović, Milica
AU  - Bulajic, Aleksandra
AU  - Ristic, Danijela
AU  - Krstic, Branka
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1545
AB  - BACKGROUND: Higher plants possess several mechanisms of defense against plant pathogens. Proteins actively synthesized in response to those stresses are called defense-related proteins which, among others, include certain protease inhibitors. It is of particular relevance to investigate plant natural defense mechanisms for pathogen control which include cystatinsspecific inhibitors of cysteine proteases. RESULTS: In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. Immuno-tissue print results indicated that CPI is most abundant in the outer layer of pericarp, near the peel, and the inner most part of the pulpsites where it could act as a natural barrier against pathogens entering the fruit. The purified protein (15 mu mol L-1) showed antifungal activity against two phytopathogenic fungi (Alternaria radicina and Botrytis cinerea) by inhibiting fungal spore germination. In vivo, CPI (10 mu mol L-1) was able to prevent artificial infection of apple and carrot with spore suspension of B. cinerea and A. radicina, respectively. It also exerted activity on both intracellular and fermentation fluid proteinases. CONCLUSION: Identification and characterization of plant defense molecules is the first step towards creation of improved methods for pathogen control based on naturally occurring molecules. Copyright (c) 2012 Society of Chemical Industry
PB  - Wiley-Blackwell, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit
VL  - 92
IS  - 15
SP  - 3072
EP  - 3078
DO  - 10.1002/jsfa.5728
UR  - Kon_2376
ER  - 
@article{
author = "Popović, Milica and Bulajic, Aleksandra and Ristic, Danijela and Krstic, Branka and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "BACKGROUND: Higher plants possess several mechanisms of defense against plant pathogens. Proteins actively synthesized in response to those stresses are called defense-related proteins which, among others, include certain protease inhibitors. It is of particular relevance to investigate plant natural defense mechanisms for pathogen control which include cystatinsspecific inhibitors of cysteine proteases. RESULTS: In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. Immuno-tissue print results indicated that CPI is most abundant in the outer layer of pericarp, near the peel, and the inner most part of the pulpsites where it could act as a natural barrier against pathogens entering the fruit. The purified protein (15 mu mol L-1) showed antifungal activity against two phytopathogenic fungi (Alternaria radicina and Botrytis cinerea) by inhibiting fungal spore germination. In vivo, CPI (10 mu mol L-1) was able to prevent artificial infection of apple and carrot with spore suspension of B. cinerea and A. radicina, respectively. It also exerted activity on both intracellular and fermentation fluid proteinases. CONCLUSION: Identification and characterization of plant defense molecules is the first step towards creation of improved methods for pathogen control based on naturally occurring molecules. Copyright (c) 2012 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit",
volume = "92",
number = "15",
pages = "3072-3078",
doi = "10.1002/jsfa.5728",
url = "Kon_2376"
}
Popović, M., Bulajic, A., Ristic, D., Krstic, B., Jankov, R. M.,& Gavrović-Jankulović, M.. (2012). In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Hoboken., 92(15), 3072-3078.
https://doi.org/10.1002/jsfa.5728
Kon_2376
Popović M, Bulajic A, Ristic D, Krstic B, Jankov RM, Gavrović-Jankulović M. In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit. in Journal of the Science of Food and Agriculture. 2012;92(15):3072-3078.
doi:10.1002/jsfa.5728
Kon_2376 .
Popović, Milica, Bulajic, Aleksandra, Ristic, Danijela, Krstic, Branka, Jankov, Ratko M., Gavrović-Jankulović, Marija, "In vitro and in vivo antifungal properties of cysteine proteinase inhibitor from green kiwifruit" in Journal of the Science of Food and Agriculture, 92, no. 15 (2012):3072-3078,
https://doi.org/10.1002/jsfa.5728 .,
Kon_2376 .
11
12
14

One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite

Dimitrijević, Aleksandra; Veličković, Dušan; Bihelović, Filip; Bezbradica, Dejan; Jankov, Ratko M.; Milosavić, Nenad

(Elsevier Sci Ltd, Oxford, 2012)

TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1264
AB  - Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite
VL  - 107
SP  - 358
EP  - 362
DO  - 10.1016/j.biortech.2011.11.077
UR  - Kon_2287
ER  - 
@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bihelović, Filip and Bezbradica, Dejan and Jankov, Ratko M. and Milosavić, Nenad",
year = "2012",
abstract = "Lipase A from Candida antarctica (CAL A) was purified to apparent homogeneity in a single step using hydroxyapatite (HAP) chromatography. CAL A bound to HAP was eluted with 10 mM Na-phosphate buffer, pH 7.0 containing 0.5% Triton X-100. The protocol resulted in a 3.74-fold purification with 94.7% final recovery and 400.83 U/mg specific activity. Silver staining after SDS-PAGE revealed the presence a single band of 45 kDa. The enzyme exhibited a temperature optimum of 60 degrees C, was unaffected by monovalent metal ions, but was destabilized by divalent metal ions (Zn2+, Ca2+, Mg2+, Cu2+, Mn2+) and stimulated by 50 mM Fe2+. Detergents at 0.1% concentrations did not affect lipase activity. Except for Triton X-100, detergent concentrations of 1% had a destabilizing effect. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite",
volume = "107",
pages = "358-362",
doi = "10.1016/j.biortech.2011.11.077",
url = "Kon_2287"
}
Dimitrijević, A., Veličković, D., Bihelović, F., Bezbradica, D., Jankov, R. M.,& Milosavić, N.. (2012). One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 107, 358-362.
https://doi.org/10.1016/j.biortech.2011.11.077
Kon_2287
Dimitrijević A, Veličković D, Bihelović F, Bezbradica D, Jankov RM, Milosavić N. One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite. in Bioresource Technology. 2012;107:358-362.
doi:10.1016/j.biortech.2011.11.077
Kon_2287 .
Dimitrijević, Aleksandra, Veličković, Dušan, Bihelović, Filip, Bezbradica, Dejan, Jankov, Ratko M., Milosavić, Nenad, "One-step, inexpensive high yield strategy for Candida antarctica lipase A isolation using hydroxyapatite" in Bioresource Technology, 107 (2012):358-362,
https://doi.org/10.1016/j.biortech.2011.11.077 .,
Kon_2287 .
16
14
18

Isolation of functional total RNA from Tilia cordata leaves and pollen

Ognjenović, Jana; Tantoush, Ziyad Omar; Jankov, Ratko M.; Ćirković-Veličković, Tanja; Vukmirica, Jelena

(Serbian Chemical Soc, Belgrade, 2012)

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Tantoush, Ziyad Omar
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
AU  - Vukmirica, Jelena
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1531
AB  - The conditions required for the isolation of high quality total RNA from European linden (Tilia cordata) leaves and pollen were determined. Pure total RNA was isolated from linden leaves utilizing a Qiagen plant mini kit, while the total RNA isolated from linden pollen using this method was degraded. Successful isolation of total RNA from both linden pollen and leaves, however, was achieved following TRIzol (TM) preparation of the total RNA. The total RNA isolated using TRIzol (TM) was contaminated with genomic DNA but treatment with the enzyme DNase, in solution or on-column, efficiently removed the genomic DNA. Furthermore, the conditions for the elimination of genomic DNA contamination on-column and isolation of pure total RNA from leaves were optimized. The isolated total RNA from both leaves and pollen was used successfully in first-and second-strand cDNA synthesis reactions and in a reverse transcription polymerase chain reaction (RT-PCR), demonstrating that the total RNA isolated using this method was functional. In conclusion, pure and functional total RNA from T. cordata leaves and pollen (27.8 +/- 7.9 mu g g(-1) leaves; 25.7 +/- 1.1 mu g g(-1) pollen) could be obtained and was suitable for application in further molecular biology studies.
AB  - Uspostavljeni su uslovi za izolovanje ukupne RNK iz lišća i polena evropske lipe (Tilia cordata). Korišćenjem komercijalno dostupnog pribora za izolovanje RNK iz biljaka izolovana je čista ukupna RNK iz lišća lipe, dok je korišćenjem iste metode dobijena degradirana RNK iz polena lipe. Uspešno izolovanje RNK iz lišća i polena je dobijeno korišćenjem TRIzol reagensa. RNK izolovana ovim metodom je kontaminirana genomskom DNK, koja je uspešno eliminisana korišćenjem enzima DNaze. Dalje su optimizovani i uslovi uklanjanja genomske DNK pomoću DNaze. Izolovana ukupna RNK iz oba izvora je dalje uspešno iskorišćena za sintezu prvog i drugog lanca klonske DNK, kao i u reverzno-transkriptivnoj PCR reakciji, dokazujući time da je korišćenjem ovog metoda izolovana funkcionalna ukupna RNK. U zaključku, dobijena je čista i funkcionalna RNK iz lišća i polena T. cordata (27,8±7,9 μg g-1 lišća; 25,7±1,1 μg g-1 polena) koja se može koristiti u daljim molekularno-biološkim istraživanjima.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Isolation of functional total RNA from Tilia cordata leaves and pollen
T1  - Izolovanje funkcionalne ukupne RNK iz lišća i polena lipe (Tilia cordata)
VL  - 77
IS  - 8
SP  - 1003
EP  - 1012
DO  - 10.2298/JSC111130018O
UR  - Kon_2362
ER  - 
@article{
author = "Ognjenović, Jana and Tantoush, Ziyad Omar and Jankov, Ratko M. and Ćirković-Veličković, Tanja and Vukmirica, Jelena",
year = "2012",
abstract = "The conditions required for the isolation of high quality total RNA from European linden (Tilia cordata) leaves and pollen were determined. Pure total RNA was isolated from linden leaves utilizing a Qiagen plant mini kit, while the total RNA isolated from linden pollen using this method was degraded. Successful isolation of total RNA from both linden pollen and leaves, however, was achieved following TRIzol (TM) preparation of the total RNA. The total RNA isolated using TRIzol (TM) was contaminated with genomic DNA but treatment with the enzyme DNase, in solution or on-column, efficiently removed the genomic DNA. Furthermore, the conditions for the elimination of genomic DNA contamination on-column and isolation of pure total RNA from leaves were optimized. The isolated total RNA from both leaves and pollen was used successfully in first-and second-strand cDNA synthesis reactions and in a reverse transcription polymerase chain reaction (RT-PCR), demonstrating that the total RNA isolated using this method was functional. In conclusion, pure and functional total RNA from T. cordata leaves and pollen (27.8 +/- 7.9 mu g g(-1) leaves; 25.7 +/- 1.1 mu g g(-1) pollen) could be obtained and was suitable for application in further molecular biology studies., Uspostavljeni su uslovi za izolovanje ukupne RNK iz lišća i polena evropske lipe (Tilia cordata). Korišćenjem komercijalno dostupnog pribora za izolovanje RNK iz biljaka izolovana je čista ukupna RNK iz lišća lipe, dok je korišćenjem iste metode dobijena degradirana RNK iz polena lipe. Uspešno izolovanje RNK iz lišća i polena je dobijeno korišćenjem TRIzol reagensa. RNK izolovana ovim metodom je kontaminirana genomskom DNK, koja je uspešno eliminisana korišćenjem enzima DNaze. Dalje su optimizovani i uslovi uklanjanja genomske DNK pomoću DNaze. Izolovana ukupna RNK iz oba izvora je dalje uspešno iskorišćena za sintezu prvog i drugog lanca klonske DNK, kao i u reverzno-transkriptivnoj PCR reakciji, dokazujući time da je korišćenjem ovog metoda izolovana funkcionalna ukupna RNK. U zaključku, dobijena je čista i funkcionalna RNK iz lišća i polena T. cordata (27,8±7,9 μg g-1 lišća; 25,7±1,1 μg g-1 polena) koja se može koristiti u daljim molekularno-biološkim istraživanjima.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation of functional total RNA from Tilia cordata leaves and pollen, Izolovanje funkcionalne ukupne RNK iz lišća i polena lipe (Tilia cordata)",
volume = "77",
number = "8",
pages = "1003-1012",
doi = "10.2298/JSC111130018O",
url = "Kon_2362"
}
Ognjenović, J., Tantoush, Z. O., Jankov, R. M., Ćirković-Veličković, T.,& Vukmirica, J.. (2012). Isolation of functional total RNA from Tilia cordata leaves and pollen. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(8), 1003-1012.
https://doi.org/10.2298/JSC111130018O
Kon_2362
Ognjenović J, Tantoush ZO, Jankov RM, Ćirković-Veličković T, Vukmirica J. Isolation of functional total RNA from Tilia cordata leaves and pollen. in Journal of the Serbian Chemical Society. 2012;77(8):1003-1012.
doi:10.2298/JSC111130018O
Kon_2362 .
Ognjenović, Jana, Tantoush, Ziyad Omar, Jankov, Ratko M., Ćirković-Veličković, Tanja, Vukmirica, Jelena, "Isolation of functional total RNA from Tilia cordata leaves and pollen" in Journal of the Serbian Chemical Society, 77, no. 8 (2012):1003-1012,
https://doi.org/10.2298/JSC111130018O .,
Kon_2362 .

A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae

Veličković, Dušan; Dimitrijević, Aleksandra; Bihelović, Filip; Bezbradica, Dejan; Jankov, Ratko M.; Milosavić, Nenad

(Elsevier Sci Ltd, Oxford, 2011)

TY  - JOUR
AU  - Veličković, Dušan
AU  - Dimitrijević, Aleksandra
AU  - Bihelović, Filip
AU  - Bezbradica, Dejan
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1186
AB  - In this report, alpha-isosalicin, a potent anticoagulant and skin whitening agent, was synthesized by a highly efficient chemoselective and diastereoselective reaction, catalyzed by maltase from bakers' yeast (Saccharomyces cerevisiae). The highest yield of this one-step transglucosylation reaction was achieved with 50 mM of salicyl alcohol as a glucose acceptor. The key reaction factors were optimized using response surface methodology (RSM) with an enzyme concentration of 10 U/mL. The optimum temperature of the reaction was determined as 36.5 degrees C, the optimal maltose concentration was 40% (w/v), the optimal pH was 6.5, and the optimal reaction time was 16 h. Under these conditions 75% of alpha-isosalicin was obtained, with a yield of 10 g/L, and no by product formation was observed.
PB  - Elsevier Sci Ltd, Oxford
T2  - Process Biochemistry
T1  - A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae
VL  - 46
IS  - 8
SP  - 1698
EP  - 1702
DO  - 10.1016/j.procbio.2011.05.007
UR  - Kon_2208
ER  - 
@article{
author = "Veličković, Dušan and Dimitrijević, Aleksandra and Bihelović, Filip and Bezbradica, Dejan and Jankov, Ratko M. and Milosavić, Nenad",
year = "2011",
abstract = "In this report, alpha-isosalicin, a potent anticoagulant and skin whitening agent, was synthesized by a highly efficient chemoselective and diastereoselective reaction, catalyzed by maltase from bakers' yeast (Saccharomyces cerevisiae). The highest yield of this one-step transglucosylation reaction was achieved with 50 mM of salicyl alcohol as a glucose acceptor. The key reaction factors were optimized using response surface methodology (RSM) with an enzyme concentration of 10 U/mL. The optimum temperature of the reaction was determined as 36.5 degrees C, the optimal maltose concentration was 40% (w/v), the optimal pH was 6.5, and the optimal reaction time was 16 h. Under these conditions 75% of alpha-isosalicin was obtained, with a yield of 10 g/L, and no by product formation was observed.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Process Biochemistry",
title = "A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae",
volume = "46",
number = "8",
pages = "1698-1702",
doi = "10.1016/j.procbio.2011.05.007",
url = "Kon_2208"
}
Veličković, D., Dimitrijević, A., Bihelović, F., Bezbradica, D., Jankov, R. M.,& Milosavić, N.. (2011). A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae. in Process Biochemistry
Elsevier Sci Ltd, Oxford., 46(8), 1698-1702.
https://doi.org/10.1016/j.procbio.2011.05.007
Kon_2208
Veličković D, Dimitrijević A, Bihelović F, Bezbradica D, Jankov RM, Milosavić N. A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae. in Process Biochemistry. 2011;46(8):1698-1702.
doi:10.1016/j.procbio.2011.05.007
Kon_2208 .
Veličković, Dušan, Dimitrijević, Aleksandra, Bihelović, Filip, Bezbradica, Dejan, Jankov, Ratko M., Milosavić, Nenad, "A highly efficient diastereoselective synthesis of alpha-isosalicin by maltase from Saccharomyces cerevisiae" in Process Biochemistry, 46, no. 8 (2011):1698-1702,
https://doi.org/10.1016/j.procbio.2011.05.007 .,
Kon_2208 .
9
9
11

Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents

Dimitrijević, Aleksandra; Veličković, Dušan; Bezbradica, Dejan; Bihelović, Filip; Jankov, Ratko M.; Milosavić, Nenad

(Serbian Chemical Soc, Belgrade, 2011)

TY  - JOUR
AU  - Dimitrijević, Aleksandra
AU  - Veličković, Dušan
AU  - Bezbradica, Dejan
AU  - Bihelović, Filip
AU  - Jankov, Ratko M.
AU  - Milosavić, Nenad
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1198
AB  - The production of lipase from Pseudozyma aphidis (DSM 70725) was determined in six different media. The highest lipase production was observed in a medium with glucose as the sole carbon source, and yeast extract and sodium nitrate as the nitrogen sources. The time course studies of growth and lipase production in the optimal medium revealed that the highest lipase production was achieved at the end of the log phase of growth, reaching the value of 35.0 U cm(-3) in the fifth day of cultivation. The effects of various polar, water-miscible, organic solvents on the activity and stability of the crude lipase produced by P. aphidis were evaluated. The hydrolytic activity of the crude lipase towards p-nitrophenyl palmitate (p-NPP) in aqueous media and in organic solvents was determined, using the same spectrophotometric assay in both the aqueous and organic media. The crude lipase preparation exhibited activity towards p-NPP only in acetone and acetonitrile, while the lipase was stable only in acetone, with 23 % residual activity after 24 h of incubation. These results suggested that lipase from P. aphidis can be used as a biocatalyst for potential applications in such organic solvents.
AB  - Proizvodnja lipaze iz Pseudozyma aphidis utvrđena je u šest različitih medijuma. Najviša proizvodnja uočena je u medijumu gde je glukoza bila izvor ugljenika, a ekstrakt kvasca i natrijum-nitrat izvori azota. Praćenjem dinamike rasta i proizvodnje lipaze u optimalnom medijumu, uočeno je da se najviša proizvodnja lipaze dostiže pred kraj logaritamske faze rasta, i dostiže vrednost od 35 U cm-3 u petom danu kultivacije, što je četri puta veća proizvodnja od one do sada prijavljene u literaturi. Utvrđen je efekat različitih polarnih organskih rastvarača, mešljivih sa vodom, na aktivnost i stabilnost lipaze iz P. aphidis. Hidrolitička aktivnost lipaze prema para-nitrofenil-palmitatu (p-NPP-u) u vo- denoj sredini i organskim rastvaračima utvrđena je upotrebom istog spektrofotometrijskog testa. Pokazano je da lipaza ima aktivnost prema p-NPP-u samo u acetonu i acetonitrilu, dok je enzim stabilan jedino u acetonu i zadržava 23% aktivnosti nakon 24 časa inkubacije. Dobijeni rezultati ukazuju da lipaza iz P. aphidis može biti korišćena kao biokatalizator za potencijalne primene u acetonu kao medijumu.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents
T1  - Proizvodnja lipaze iz Pseudozyma aphidis i utvrđivanje aktivnosti i stabilnosti lipaze u polarnim organskim rastvaračima
VL  - 76
IS  - 8
SP  - 1081
EP  - 1092
DO  - 10.2298/JSC110428096D
UR  - Kon_2220
ER  - 
@article{
author = "Dimitrijević, Aleksandra and Veličković, Dušan and Bezbradica, Dejan and Bihelović, Filip and Jankov, Ratko M. and Milosavić, Nenad",
year = "2011",
abstract = "The production of lipase from Pseudozyma aphidis (DSM 70725) was determined in six different media. The highest lipase production was observed in a medium with glucose as the sole carbon source, and yeast extract and sodium nitrate as the nitrogen sources. The time course studies of growth and lipase production in the optimal medium revealed that the highest lipase production was achieved at the end of the log phase of growth, reaching the value of 35.0 U cm(-3) in the fifth day of cultivation. The effects of various polar, water-miscible, organic solvents on the activity and stability of the crude lipase produced by P. aphidis were evaluated. The hydrolytic activity of the crude lipase towards p-nitrophenyl palmitate (p-NPP) in aqueous media and in organic solvents was determined, using the same spectrophotometric assay in both the aqueous and organic media. The crude lipase preparation exhibited activity towards p-NPP only in acetone and acetonitrile, while the lipase was stable only in acetone, with 23 % residual activity after 24 h of incubation. These results suggested that lipase from P. aphidis can be used as a biocatalyst for potential applications in such organic solvents., Proizvodnja lipaze iz Pseudozyma aphidis utvrđena je u šest različitih medijuma. Najviša proizvodnja uočena je u medijumu gde je glukoza bila izvor ugljenika, a ekstrakt kvasca i natrijum-nitrat izvori azota. Praćenjem dinamike rasta i proizvodnje lipaze u optimalnom medijumu, uočeno je da se najviša proizvodnja lipaze dostiže pred kraj logaritamske faze rasta, i dostiže vrednost od 35 U cm-3 u petom danu kultivacije, što je četri puta veća proizvodnja od one do sada prijavljene u literaturi. Utvrđen je efekat različitih polarnih organskih rastvarača, mešljivih sa vodom, na aktivnost i stabilnost lipaze iz P. aphidis. Hidrolitička aktivnost lipaze prema para-nitrofenil-palmitatu (p-NPP-u) u vo- denoj sredini i organskim rastvaračima utvrđena je upotrebom istog spektrofotometrijskog testa. Pokazano je da lipaza ima aktivnost prema p-NPP-u samo u acetonu i acetonitrilu, dok je enzim stabilan jedino u acetonu i zadržava 23% aktivnosti nakon 24 časa inkubacije. Dobijeni rezultati ukazuju da lipaza iz P. aphidis može biti korišćena kao biokatalizator za potencijalne primene u acetonu kao medijumu.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents, Proizvodnja lipaze iz Pseudozyma aphidis i utvrđivanje aktivnosti i stabilnosti lipaze u polarnim organskim rastvaračima",
volume = "76",
number = "8",
pages = "1081-1092",
doi = "10.2298/JSC110428096D",
url = "Kon_2220"
}
Dimitrijević, A., Veličković, D., Bezbradica, D., Bihelović, F., Jankov, R. M.,& Milosavić, N.. (2011). Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(8), 1081-1092.
https://doi.org/10.2298/JSC110428096D
Kon_2220
Dimitrijević A, Veličković D, Bezbradica D, Bihelović F, Jankov RM, Milosavić N. Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents. in Journal of the Serbian Chemical Society. 2011;76(8):1081-1092.
doi:10.2298/JSC110428096D
Kon_2220 .
Dimitrijević, Aleksandra, Veličković, Dušan, Bezbradica, Dejan, Bihelović, Filip, Jankov, Ratko M., Milosavić, Nenad, "Production of lipase from Pseudozyma aphidis and determination of the activity and stability of the crude lipase preparation in polar organic solvents" in Journal of the Serbian Chemical Society, 76, no. 8 (2011):1081-1092,
https://doi.org/10.2298/JSC110428096D .,
Kon_2220 .
10
11
14

Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase

Velickovic, D. V.; Dimitrijevic, A. S.; Bihelović, Filip; Jankov, Ratko M.; Milosavic, N.

(Maik Nauka/Interperiodica/Springer, New York, 2011)

TY  - JOUR
AU  - Velickovic, D. V.
AU  - Dimitrijevic, A. S.
AU  - Bihelović, Filip
AU  - Jankov, Ratko M.
AU  - Milosavic, N.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1231
AB  - One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.
PB  - Maik Nauka/Interperiodica/Springer, New York
T2  - Russian Journal of Physical Chemistry A
T1  - Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase
VL  - 85
IS  - 13
SP  - 2317
EP  - 2321
DO  - 10.1134/S0036024411130346
UR  - Kon_2253
ER  - 
@article{
author = "Velickovic, D. V. and Dimitrijevic, A. S. and Bihelović, Filip and Jankov, Ratko M. and Milosavic, N.",
year = "2011",
abstract = "One of the key elements for understanding enzyme reactions is determination of its kinetic parameters. Since transglucosylation is kinetically controlled reaction, besides the reaction of synthesis, very important is the reaction of enzymatic hydrolysis of created product. Therefore, in this study, kinetic parameters for synthesis and secondary hydrolysis of pharmacologically active alpha isosalicin by baker's yeast maltase were calculated, and it was shown that specifity of maltase for hydrolysis is approximately 150 times higher then for synthesis.",
publisher = "Maik Nauka/Interperiodica/Springer, New York",
journal = "Russian Journal of Physical Chemistry A",
title = "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase",
volume = "85",
number = "13",
pages = "2317-2321",
doi = "10.1134/S0036024411130346",
url = "Kon_2253"
}
Velickovic, D. V., Dimitrijevic, A. S., Bihelović, F., Jankov, R. M.,& Milosavic, N.. (2011). Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A
Maik Nauka/Interperiodica/Springer, New York., 85(13), 2317-2321.
https://doi.org/10.1134/S0036024411130346
Kon_2253
Velickovic DV, Dimitrijevic AS, Bihelović F, Jankov RM, Milosavic N. Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase. in Russian Journal of Physical Chemistry A. 2011;85(13):2317-2321.
doi:10.1134/S0036024411130346
Kon_2253 .
Velickovic, D. V., Dimitrijevic, A. S., Bihelović, Filip, Jankov, Ratko M., Milosavic, N., "Study of the kinetic parameters for synthesis and hydrolysis of pharmacologically active salicin isomer catalyzed by baker's yeast maltase" in Russian Journal of Physical Chemistry A, 85, no. 13 (2011):2317-2321,
https://doi.org/10.1134/S0036024411130346 .,
Kon_2253 .
4
4
4

Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols

Tantoush, Ziyad; Mihajlovic, Luka; Kravić, Bojana; Ognjenović, Jana; Jankov, Ratko M.; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Serbian Chemical Soc, Belgrade, 2011)

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Mihajlovic, Luka
AU  - Kravić, Bojana
AU  - Ognjenović, Jana
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1174
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow's milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the biphasal pepsin pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders.
AB  - β-Laktoglobulin (BLG) je važan nutrijent mlečnih proizvoda i važan alergen kod alergija na kravlje mleko. Cilj ove studije je bilo ispitivanje potencijala lakaze da unakrsno poveže BLG u prisustvu fenolnog ekstrakta jabuke (APE), kao i karakterizacija dobijenih proizvoda sa aspekta njihove digestibilnosti pepsinom i pankreatinom. Kompozicija fenola jabuke korišćenih za unakrsno povezivanje određena je pomoću LC-ESI-MS. Fenolni ekstrakt jabuke sadrži znatne količine glikozida kvercetina, katehine i hlorogensku kiselinu. BLG je unakrsno povezan lakazom u prisustvu fenola jabuke, pri čemu je polimerizacija učinila BLG nerastvornim u reakcionoj smeši. SDS-PAGE analiza pokazala je da reakciona smeša sadrži heterogenu smešu velikih molekulskih masa (unakrsno povezan BLG), kao i deo zaostalog monomernog BLG. Enzimsko procesovanje BLG lakazom, u prisustvu polifenola jabuke kao medijatora, može smanjiti bifaznu pepsin-pankreatinsku digestibilnost kako monomernog, tako i unakrsno povezanog BLG, i na taj način smanjiti njegovu nutritivnu vrednost. Takođe, smanjena digestibilnost BLG može smanjiti njegov alergeni potencijal. Polifenoli jabuke mogu se koristiti za kreiranje novih, funkcionalnijih prehrambenih proizvoda, dizajniranih za prevenciju kako gojaznosti, tako i bolesti vezanih za preosetljivost.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols
T1  - Digestibilnost β-laktoglobulina nakon njegovog unakrsnog povezivanja dejstvom lakaze iz Trametes versicolor i polifenola iz jabuke
VL  - 76
IS  - 6
SP  - 847
EP  - 855
DO  - 10.2298/JSC101201077T
UR  - Kon_2196
ER  - 
@article{
author = "Tantoush, Ziyad and Mihajlovic, Luka and Kravić, Bojana and Ognjenović, Jana and Jankov, Ratko M. and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow's milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the biphasal pepsin pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders., β-Laktoglobulin (BLG) je važan nutrijent mlečnih proizvoda i važan alergen kod alergija na kravlje mleko. Cilj ove studije je bilo ispitivanje potencijala lakaze da unakrsno poveže BLG u prisustvu fenolnog ekstrakta jabuke (APE), kao i karakterizacija dobijenih proizvoda sa aspekta njihove digestibilnosti pepsinom i pankreatinom. Kompozicija fenola jabuke korišćenih za unakrsno povezivanje određena je pomoću LC-ESI-MS. Fenolni ekstrakt jabuke sadrži znatne količine glikozida kvercetina, katehine i hlorogensku kiselinu. BLG je unakrsno povezan lakazom u prisustvu fenola jabuke, pri čemu je polimerizacija učinila BLG nerastvornim u reakcionoj smeši. SDS-PAGE analiza pokazala je da reakciona smeša sadrži heterogenu smešu velikih molekulskih masa (unakrsno povezan BLG), kao i deo zaostalog monomernog BLG. Enzimsko procesovanje BLG lakazom, u prisustvu polifenola jabuke kao medijatora, može smanjiti bifaznu pepsin-pankreatinsku digestibilnost kako monomernog, tako i unakrsno povezanog BLG, i na taj način smanjiti njegovu nutritivnu vrednost. Takođe, smanjena digestibilnost BLG može smanjiti njegov alergeni potencijal. Polifenoli jabuke mogu se koristiti za kreiranje novih, funkcionalnijih prehrambenih proizvoda, dizajniranih za prevenciju kako gojaznosti, tako i bolesti vezanih za preosetljivost.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols, Digestibilnost β-laktoglobulina nakon njegovog unakrsnog povezivanja dejstvom lakaze iz Trametes versicolor i polifenola iz jabuke",
volume = "76",
number = "6",
pages = "847-855",
doi = "10.2298/JSC101201077T",
url = "Kon_2196"
}
Tantoush, Z., Mihajlovic, L., Kravić, B., Ognjenović, J., Jankov, R. M., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2011). Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(6), 847-855.
https://doi.org/10.2298/JSC101201077T
Kon_2196
Tantoush Z, Mihajlovic L, Kravić B, Ognjenović J, Jankov RM, Ćirković-Veličković T, Stanić-Vučinić D. Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols. in Journal of the Serbian Chemical Society. 2011;76(6):847-855.
doi:10.2298/JSC101201077T
Kon_2196 .
Tantoush, Ziyad, Mihajlovic, Luka, Kravić, Bojana, Ognjenović, Jana, Jankov, Ratko M., Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols" in Journal of the Serbian Chemical Society, 76, no. 6 (2011):847-855,
https://doi.org/10.2298/JSC101201077T .,
Kon_2196 .
6
4
5
6

The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2)

Seatovic, Svetlana L.; Jovanović-Novaković, Jelena S.; Zavisic, Gordana N.; Radulovic, Zeljka C.; Gavrović-Jankulović, Marija; Jankov, Ratko M.

(Serbian Chemical Soc, Belgrade, 2011)

TY  - JOUR
AU  - Seatovic, Svetlana L.
AU  - Jovanović-Novaković, Jelena S.
AU  - Zavisic, Gordana N.
AU  - Radulovic, Zeljka C.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1350
AB  - The aim of this study was the partial characterization of the antimicrobial peptide bacteriocin G, produced by probiotic bacteria Lactobacillus plantarum G(2), which was isolated from a clinical sample of a healthy person. Antimicrobial substance was secreted in the supernatant of an L. plantarum G(2) culture, and showed a diverse spectrum of antimicrobial activity of all the tested strains of the genera Lactobacillus and the pathogenic bacteria Staphylococcus aureus and Salmonella abony. Isoclectric focusing revealed that bacteriocin G(2) is a cationic peptide (pI about 10) with a molecular mass of 2.2 kDa according to tricine sodium dodecyl sulphate polyacrylamide gel electrophoresis, SDS-PAGE. The antimicrobial activity of bactcriocin G(2) was diminished by the proteolytic action of trypsin and proteinase K. Bacteriocin G(2) preserved its biological activity in the temperature range 40-60 degrees C (15 min), which was lost at 80 degrees C. Bacteriocin G(2) was stable in the pH range 2-9, while treatment with 1 % Tween 80 and 1 % urea resulted in increased antimicrobial activity. The probiotic strain L. plantarum G(2) produces the antimicrobial substance proteinaceous in nature with bacteriocin characteristics. Bacteriocin production is one of the key properties of probiotic bacteria with clinical potential as anti-infective agents, which will increase the likelihood of its in vivo efficacy.
AB  - Cilj ovog istraživanja je bila parcijalna karakterizacija antimikrobnog peptida iz probiotske bakterija Lactobacillus plantarum G2 izolovane iz kliničkog uzorka zdrave osobe. Antimikrobno jedinjenje iz L. plantarum G2, označeno kao bakteriocin G2, dobijeno iz supernatanta bakterijske kulture, pokazalo je širok spektar antimikrobne aktivnosti, inhibirajići rast svih ispitivanh vrsta roda Lactobacillus, kao i patogenih bakterija Staphylococcus aureus i Salmonella abony. Bakteriocin G2 je osetljiv na proteolitičko dejstvo tripsina i proteinaze K. Antimikrobna aktivnost je stabilna u opsegu 40-60°C (15 min), ali se gubi na temperaturi od 80°C. Ustanovljeno je da je bakteriocin stabilan na pH vrednostima između 2 i 9. Dejstvo Tween-a 80 i uree je dovelo do povećane inhibitorne aktivnosti. Prema IEF, bakteriocin G2 je katjonski protein, sa pI vrednošću oko 10, a molekulaska masa određena na osnovu tricin-SDS-PAGE je 2,2 kDa. Probiotski soj L plantarum G2 produkuje antimikrobno jedinjenje proteinske strukture sa karakteristikama bakteriocina. Sinteza bakteriocina je jedna od ključnih osobina probiotskih bakterija koje imaju klinički potencijal kao antiinfektivni agensi, jer značajno povećava verovatnoću njihove in vivo efikasnosti.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2)
T1  - Parcijalna karakterizacija antibakterijskog peptida koji proizvodi probiotska bakterija Lactobacillus plantarum G2
VL  - 76
IS  - 5
SP  - 699
EP  - 707
DO  - 10.2298/JSC100605060S
UR  - Kon_2188
ER  - 
@article{
author = "Seatovic, Svetlana L. and Jovanović-Novaković, Jelena S. and Zavisic, Gordana N. and Radulovic, Zeljka C. and Gavrović-Jankulović, Marija and Jankov, Ratko M.",
year = "2011",
abstract = "The aim of this study was the partial characterization of the antimicrobial peptide bacteriocin G, produced by probiotic bacteria Lactobacillus plantarum G(2), which was isolated from a clinical sample of a healthy person. Antimicrobial substance was secreted in the supernatant of an L. plantarum G(2) culture, and showed a diverse spectrum of antimicrobial activity of all the tested strains of the genera Lactobacillus and the pathogenic bacteria Staphylococcus aureus and Salmonella abony. Isoclectric focusing revealed that bacteriocin G(2) is a cationic peptide (pI about 10) with a molecular mass of 2.2 kDa according to tricine sodium dodecyl sulphate polyacrylamide gel electrophoresis, SDS-PAGE. The antimicrobial activity of bactcriocin G(2) was diminished by the proteolytic action of trypsin and proteinase K. Bacteriocin G(2) preserved its biological activity in the temperature range 40-60 degrees C (15 min), which was lost at 80 degrees C. Bacteriocin G(2) was stable in the pH range 2-9, while treatment with 1 % Tween 80 and 1 % urea resulted in increased antimicrobial activity. The probiotic strain L. plantarum G(2) produces the antimicrobial substance proteinaceous in nature with bacteriocin characteristics. Bacteriocin production is one of the key properties of probiotic bacteria with clinical potential as anti-infective agents, which will increase the likelihood of its in vivo efficacy., Cilj ovog istraživanja je bila parcijalna karakterizacija antimikrobnog peptida iz probiotske bakterija Lactobacillus plantarum G2 izolovane iz kliničkog uzorka zdrave osobe. Antimikrobno jedinjenje iz L. plantarum G2, označeno kao bakteriocin G2, dobijeno iz supernatanta bakterijske kulture, pokazalo je širok spektar antimikrobne aktivnosti, inhibirajići rast svih ispitivanh vrsta roda Lactobacillus, kao i patogenih bakterija Staphylococcus aureus i Salmonella abony. Bakteriocin G2 je osetljiv na proteolitičko dejstvo tripsina i proteinaze K. Antimikrobna aktivnost je stabilna u opsegu 40-60°C (15 min), ali se gubi na temperaturi od 80°C. Ustanovljeno je da je bakteriocin stabilan na pH vrednostima između 2 i 9. Dejstvo Tween-a 80 i uree je dovelo do povećane inhibitorne aktivnosti. Prema IEF, bakteriocin G2 je katjonski protein, sa pI vrednošću oko 10, a molekulaska masa određena na osnovu tricin-SDS-PAGE je 2,2 kDa. Probiotski soj L plantarum G2 produkuje antimikrobno jedinjenje proteinske strukture sa karakteristikama bakteriocina. Sinteza bakteriocina je jedna od ključnih osobina probiotskih bakterija koje imaju klinički potencijal kao antiinfektivni agensi, jer značajno povećava verovatnoću njihove in vivo efikasnosti.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2), Parcijalna karakterizacija antibakterijskog peptida koji proizvodi probiotska bakterija Lactobacillus plantarum G2",
volume = "76",
number = "5",
pages = "699-707",
doi = "10.2298/JSC100605060S",
url = "Kon_2188"
}
Seatovic, S. L., Jovanović-Novaković, J. S., Zavisic, G. N., Radulovic, Z. C., Gavrović-Jankulović, M.,& Jankov, R. M.. (2011). The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2). in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(5), 699-707.
https://doi.org/10.2298/JSC100605060S
Kon_2188
Seatovic SL, Jovanović-Novaković JS, Zavisic GN, Radulovic ZC, Gavrović-Jankulović M, Jankov RM. The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2). in Journal of the Serbian Chemical Society. 2011;76(5):699-707.
doi:10.2298/JSC100605060S
Kon_2188 .
Seatovic, Svetlana L., Jovanović-Novaković, Jelena S., Zavisic, Gordana N., Radulovic, Zeljka C., Gavrović-Jankulović, Marija, Jankov, Ratko M., "The partial characterization of the antibacterial peptide bacteriocin G(2) produced by the probiotic bacteria Lactobacillus plantarum G(2)" in Journal of the Serbian Chemical Society, 76, no. 5 (2011):699-707,
https://doi.org/10.2298/JSC100605060S .,
Kon_2188 .
5
7
7

Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy

Popović, Milica; Milovanovic, Mina; Burazer, Lidija M.; Vuckovic, Olga; Hoffmann-Sommergruber, Karin; Knulst, Andre C.; Lindner, Buko; Petersen, Arnd; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-V C H Verlag Gmbh, Weinheim, 2010)

TY  - JOUR
AU  - Popović, Milica
AU  - Milovanovic, Mina
AU  - Burazer, Lidija M.
AU  - Vuckovic, 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
UR  - Kon_2068
ER  - 
@article{
author = "Popović, Milica and Milovanovic, Mina and Burazer, Lidija M. and Vuckovic, 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",
url = "Kon_2068"
}
Popović, M., Milovanovic, M., Burazer, L. M., Vuckovic, 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
Kon_2068
Popović M, Milovanovic M, Burazer LM, Vuckovic 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
Kon_2068 .
Popović, Milica, Milovanovic, Mina, Burazer, Lidija M., Vuckovic, 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 .,
Kon_2068 .
10
10
10

Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed

Popović, Milica; Burazer, Lidija M.; Vuckovic, O.; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Hoboken, 2010)

TY  - CONF
AU  - Popović, Milica
AU  - Burazer, Lidija M.
AU  - Vuckovic, O.
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1468
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed
VL  - 65
SP  - 323
EP  - 323
UR  - Kon_2588
ER  - 
@conference{
author = "Popović, Milica and Burazer, Lidija M. and Vuckovic, O. and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2010",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed",
volume = "65",
pages = "323-323",
url = "Kon_2588"
}
Popović, M., Burazer, L. M., Vuckovic, O., Jankov, R. M.,& Gavrović-Jankulović, M.. (2010). Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed. in Allergy
Wiley-Blackwell, Hoboken., 65, 323-323.
Kon_2588
Popović M, Burazer LM, Vuckovic O, Jankov RM, Gavrović-Jankulović M. Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed. in Allergy. 2010;65:323-323.
Kon_2588 .
Popović, Milica, Burazer, Lidija M., Vuckovic, O., Jankov, Ratko M., Gavrović-Jankulović, Marija, "Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed" in Allergy, 65 (2010):323-323,
Kon_2588 .

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

Stojanović, Marijana M.; Živković, Irena; Petrusic, Vladimir Z.; Kosec, Dusko J.; Dimitrijevic, Rajna D.; Jankov, Ratko M.; Dimitrijevic, Ljijana A.; Gavrović-Jankulović, Marija

(Elsevier Science Bv, Amsterdam, 2010)

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
UR  - Kon_2043
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",
url = "Kon_2043"
}
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
Kon_2043
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
Kon_2043 .
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 .,
Kon_2043 .
17
17
21

Removal of N-terminal peptides from beta-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation

Stanić, Dragana; Radosavljević, Jelena; Polović, Natalija; Jadranin, Milka; Popović, Milica; Vuckovic, Olga; Burazer, Lidija M.; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2009)

TY  - JOUR
AU  - Stanić, Dragana
AU  - Radosavljević, Jelena
AU  - Polović, Natalija
AU  - Jadranin, Milka
AU  - Popović, Milica
AU  - Vuckovic, 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
UR  - Kon_2019
ER  - 
@article{
author = "Stanić, Dragana and Radosavljević, Jelena and Polović, Natalija and Jadranin, Milka and Popović, Milica and Vuckovic, 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",
url = "Kon_2019"
}
Stanić, D., Radosavljević, J., Polović, N., Jadranin, M., Popović, M., Vuckovic, 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
Kon_2019
Stanić D, Radosavljević J, Polović N, Jadranin M, Popović M, Vuckovic 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
Kon_2019 .
Stanić, Dragana, Radosavljević, Jelena, Polović, Natalija, Jadranin, Milka, Popović, Milica, Vuckovic, 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 .,
Kon_2019 .
6
8
8

Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation

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

(Wiley-Blackwell Publishing, Inc, Malden, 2009)

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
UR  - Kon_1949
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",
url = "Kon_1949"
}
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
Kon_1949
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
Kon_1949 .
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 .,
Kon_1949 .
9
9
9

Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion

Polović, Natalija; Pjanovic, Rada V.; Burazer, Lidija M.; Veličković, Sava; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(John Wiley & Sons Ltd, Chichester, 2009)

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
UR  - Kon_1941
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",
url = "Kon_1941"
}
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
Kon_1941
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
Kon_1941 .
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 .,
Kon_1941 .
17
14
17

Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy

Popović, Milica; Milovanovic, M.; Burazer, Lidija M.; Vuckovic, O.; Knulst, A.; Hoffmann-Sommergruber, K.; Lindner, B.; Petersen, A.; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-Blackwell Publishing, Inc, Malden, 2009)

TY  - CONF
AU  - Popović, Milica
AU  - Milovanovic, M.
AU  - Burazer, Lidija M.
AU  - Vuckovic, O.
AU  - Knulst, A.
AU  - Hoffmann-Sommergruber, K.
AU  - Lindner, B.
AU  - Petersen, A.
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/985
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy
VL  - 64
SP  - 270
EP  - 271
UR  - Kon_1985
ER  - 
@conference{
author = "Popović, Milica and Milovanovic, M. and Burazer, Lidija M. and Vuckovic, O. and Knulst, A. and Hoffmann-Sommergruber, K. and Lindner, B. and Petersen, A. and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy",
volume = "64",
pages = "270-271",
url = "Kon_1985"
}
Popović, M., Milovanovic, M., Burazer, L. M., Vuckovic, O., Knulst, A., Hoffmann-Sommergruber, K., Lindner, B., Petersen, A., Jankov, R. M.,& Gavrović-Jankulović, M.. (2009). Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 270-271.
Kon_1985
Popović M, Milovanovic M, Burazer LM, Vuckovic O, Knulst A, Hoffmann-Sommergruber K, Lindner B, Petersen A, Jankov RM, Gavrović-Jankulović M. Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Allergy. 2009;64:270-271.
Kon_1985 .
Popović, Milica, Milovanovic, M., Burazer, Lidija M., Vuckovic, O., Knulst, A., Hoffmann-Sommergruber, K., Lindner, B., Petersen, A., Jankov, Ratko M., Gavrović-Jankulović, Marija, "Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy" in Allergy, 64 (2009):270-271,
Kon_1985 .

The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68

Dimitrijevic, R.; Stojanovic, M.; Živković, Irena; Petersen, A.; Jankov, Ratko M.; Dimitrijevic, L.; Gavrović-Jankulović, Marija

(Wiley-Blackwell, Hoboken, 2009)

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
UR  - Kon_2028
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",
url = "Kon_2028"
}
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
Kon_2028
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
Kon_2028 .
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 .,
Kon_2028 .
6
21
20
22

Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation

Stanić, Dragana; Burazer, Lidija M.; Gavrović-Jankulović, Marija; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(Serbian Chemical Soc, Belgrade, 2009)

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
UR  - Kon_1988
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",
url = "Kon_1988"
}
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
Kon_1988
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
Kon_1988 .
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 .,
Kon_1988 .
3
3
4

Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus

Milovanovic, Katarina; Burazer, Lidija M.; Vuckovic, Olga; Atanasković-Marković, Marina; Ćirković-Veličković, Tanja; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Serbian Chemical Soc, Belgrade, 2009)

TY  - JOUR
AU  - Milovanovic, Katarina
AU  - Burazer, Lidija M.
AU  - Vuckovic, 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
UR  - Kon_1992
ER  - 
@article{
author = "Milovanovic, Katarina and Burazer, Lidija M. and Vuckovic, 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",
url = "Kon_1992"
}
Milovanovic, K., Burazer, L. M., Vuckovic, 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
Kon_1992
Milovanovic K, Burazer LM, Vuckovic 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
Kon_1992 .
Milovanovic, Katarina, Burazer, Lidija M., Vuckovic, 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 .,
Kon_1992 .
1
1

Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen

Grozdanovic, M.; Burazer, Lidija M.; Vuckovic, O.; Ćirković-Veličković, Tanja; Jankov, Ratko M.; Gavrović-Jankulović, Marija

(Wiley-Blackwell Publishing, Inc, Malden, 2009)

TY  - CONF
AU  - Grozdanovic, M.
AU  - Burazer, Lidija M.
AU  - Vuckovic, O.
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/984
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen
VL  - 64
SP  - 249
EP  - 249
UR  - Kon_1984
ER  - 
@conference{
author = "Grozdanovic, M. and Burazer, Lidija M. and Vuckovic, O. and Ćirković-Veličković, Tanja and Jankov, Ratko M. and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen",
volume = "64",
pages = "249-249",
url = "Kon_1984"
}
Grozdanovic, M., Burazer, L. M., Vuckovic, O., Ćirković-Veličković, T., Jankov, R. M.,& Gavrović-Jankulović, M.. (2009). Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 249-249.
Kon_1984
Grozdanovic M, Burazer LM, Vuckovic O, Ćirković-Veličković T, Jankov RM, Gavrović-Jankulović M. Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy. 2009;64:249-249.
Kon_1984 .
Grozdanovic, M., Burazer, Lidija M., Vuckovic, O., Ćirković-Veličković, Tanja, Jankov, Ratko M., Gavrović-Jankulović, Marija, "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen" in Allergy, 64 (2009):249-249,
Kon_1984 .

Design and modifications of allergens for improving specific immunotherapy

Ćirković-Veličković, Tanja; Jankov, Ratko M.

(2008)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko M.
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/100
AB  - Specific immunotherapy is a clinically effective causative treatment for allergic conditions. However, the reagents used for immunotherapy are crude extracts, prepared from natural sources, and as such may cause potential life-threatening anaphylactic side effects. Our increasing knowledge of mechanisms that lead to allergy and of the mechanisms of successful immunotherapy have introduced new ideas for the treatment of allergic diseases. Techniques of biochemistry and molecular biology have made it feasible to design novel therapeutic approaches for improved and safer forms of allergen-specific immunotherapy. The purpose of this review is to examine different approaches in designing novel allergen formulations for specific immunotherapy. These include chemically modified forms of allergens, genetically modified allergens (hypoallergens), hybrid allergens and allergens bearing immunostimulatory molecules, or adjuvants, which foster Th 1 immune responses. There is great interest in newly designed allergens and their derivatives to improve the efficacy and safety of allergen immunotherapy. A better understanding of immunological mechanisms and further clinical trials utilizing new allergen formulations are needed. © 2008 Bentham Science Publishers Ltd.
T2  - Inflammation and Allergy - Drug Targets
T1  - Design and modifications of allergens for improving specific immunotherapy
VL  - 7
IS  - 4
SP  - 270
EP  - 278
DO  - 10.2174/187152808786848432
UR  - Kon_1178
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Jankov, Ratko M.",
year = "2008",
abstract = "Specific immunotherapy is a clinically effective causative treatment for allergic conditions. However, the reagents used for immunotherapy are crude extracts, prepared from natural sources, and as such may cause potential life-threatening anaphylactic side effects. Our increasing knowledge of mechanisms that lead to allergy and of the mechanisms of successful immunotherapy have introduced new ideas for the treatment of allergic diseases. Techniques of biochemistry and molecular biology have made it feasible to design novel therapeutic approaches for improved and safer forms of allergen-specific immunotherapy. The purpose of this review is to examine different approaches in designing novel allergen formulations for specific immunotherapy. These include chemically modified forms of allergens, genetically modified allergens (hypoallergens), hybrid allergens and allergens bearing immunostimulatory molecules, or adjuvants, which foster Th 1 immune responses. There is great interest in newly designed allergens and their derivatives to improve the efficacy and safety of allergen immunotherapy. A better understanding of immunological mechanisms and further clinical trials utilizing new allergen formulations are needed. © 2008 Bentham Science Publishers Ltd.",
journal = "Inflammation and Allergy - Drug Targets",
title = "Design and modifications of allergens for improving specific immunotherapy",
volume = "7",
number = "4",
pages = "270-278",
doi = "10.2174/187152808786848432",
url = "Kon_1178"
}
Ćirković-Veličković, T.,& Jankov, R. M.. (2008). Design and modifications of allergens for improving specific immunotherapy. in Inflammation and Allergy - Drug Targets, 7(4), 270-278.
https://doi.org/10.2174/187152808786848432
Kon_1178
Ćirković-Veličković T, Jankov RM. Design and modifications of allergens for improving specific immunotherapy. in Inflammation and Allergy - Drug Targets. 2008;7(4):270-278.
doi:10.2174/187152808786848432
Kon_1178 .
Ćirković-Veličković, Tanja, Jankov, Ratko M., "Design and modifications of allergens for improving specific immunotherapy" in Inflammation and Allergy - Drug Targets, 7, no. 4 (2008):270-278,
https://doi.org/10.2174/187152808786848432 .,
Kon_1178 .
5
8

A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy

Popović, Milica; Burazers, L.; Atanasković-Marković, Marina; Milovanovic, M.; Ćirković-Veličković, Tanja; Petersen, A.; Jankov, Ratko M.; Becker, W.; Gavrović-Jankulović, Marija

(Blackwell Publishing, Oxford, 2008)

TY  - CONF
AU  - Popović, Milica
AU  - Burazers, L.
AU  - Atanasković-Marković, Marina
AU  - Milovanovic, M.
AU  - Ćirković-Veličković, Tanja
AU  - Petersen, A.
AU  - Jankov, Ratko M.
AU  - Becker, W.
AU  - Gavrović-Jankulović, Marija
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/941
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy
VL  - 63
SP  - 573
EP  - 573
UR  - Kon_1894
ER  - 
@conference{
author = "Popović, Milica and Burazers, L. and Atanasković-Marković, Marina and Milovanovic, M. and Ćirković-Veličković, Tanja and Petersen, A. and Jankov, Ratko M. and Becker, W. and Gavrović-Jankulović, Marija",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy",
volume = "63",
pages = "573-573",
url = "Kon_1894"
}
Popović, M., Burazers, L., Atanasković-Marković, M., Milovanovic, M., Ćirković-Veličković, T., Petersen, A., Jankov, R. M., Becker, W.,& Gavrović-Jankulović, M.. (2008). A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy. in Allergy
Blackwell Publishing, Oxford., 63, 573-573.
Kon_1894
Popović M, Burazers L, Atanasković-Marković M, Milovanovic M, Ćirković-Veličković T, Petersen A, Jankov RM, Becker W, Gavrović-Jankulović M. A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy. in Allergy. 2008;63:573-573.
Kon_1894 .
Popović, Milica, Burazers, L., Atanasković-Marković, Marina, Milovanovic, M., Ćirković-Veličković, Tanja, Petersen, A., Jankov, Ratko M., Becker, W., Gavrović-Jankulović, Marija, "A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy" in Allergy, 63 (2008):573-573,
Kon_1894 .

Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA

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.

(Wiley-Blackwell, Malden, 2008)

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
UR  - Kon_1901
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",
url = "Kon_1901"
}
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
Kon_1901
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
Kon_1901 .
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 .,
Kon_1901 .
19
16
21

Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation

Stanić, Dragana; Milovanovic, M.; Atanasković-Marković, Marina; Burazer, Lidija M.; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Malden, 2008)

TY  - CONF
AU  - Stanić, Dragana
AU  - Milovanovic, M.
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/939
PB  - Wiley-Blackwell, Malden
C3  - Allergy
T1  - Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation
VL  - 63
SP  - 496
EP  - 496
UR  - Kon_1892
ER  - 
@conference{
author = "Stanić, Dragana and Milovanovic, M. and Atanasković-Marković, Marina and Burazer, Lidija M. and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Wiley-Blackwell, Malden",
journal = "Allergy",
title = "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation",
volume = "63",
pages = "496-496",
url = "Kon_1892"
}
Stanić, D., Milovanovic, M., Atanasković-Marković, M., Burazer, L. M., Jankov, R. M.,& Ćirković-Veličković, T.. (2008). Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy
Wiley-Blackwell, Malden., 63, 496-496.
Kon_1892
Stanić D, Milovanovic M, Atanasković-Marković M, Burazer LM, Jankov RM, Ćirković-Veličković T. Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy. 2008;63:496-496.
Kon_1892 .
Stanić, Dragana, Milovanovic, M., Atanasković-Marković, Marina, Burazer, Lidija M., Jankov, Ratko M., Ćirković-Veličković, Tanja, "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation" in Allergy, 63 (2008):496-496,
Kon_1892 .

Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens

Blanusa, M.; Milovanovic, M.; Atanasković-Marković, Marina; Burazer, Lidija M.; Gavrović-Jankulović, Marija; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(Blackwell Publishing, Oxford, 2008)

TY  - CONF
AU  - Blanusa, M.
AU  - Milovanovic, M.
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/940
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens
VL  - 63
SP  - 549
EP  - 549
UR  - Kon_1893
ER  - 
@conference{
author = "Blanusa, M. and Milovanovic, M. and Atanasković-Marković, Marina and Burazer, Lidija M. and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens",
volume = "63",
pages = "549-549",
url = "Kon_1893"
}
Blanusa, M., Milovanovic, M., Atanasković-Marković, M., Burazer, L. M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2008). Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens. in Allergy
Blackwell Publishing, Oxford., 63, 549-549.
Kon_1893
Blanusa M, Milovanovic M, Atanasković-Marković M, Burazer LM, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens. in Allergy. 2008;63:549-549.
Kon_1893 .
Blanusa, M., Milovanovic, M., Atanasković-Marković, Marina, Burazer, Lidija M., Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Purification and biochemical characterisation of linden (Tilia cordata) pollen allergens" in Allergy, 63 (2008):549-549,
Kon_1893 .

Transit times of kiwi fruit proteins through rat's gastrointestinal

Polović, Natalija; Obradovic, A.; Spasic, M.; Plecas, B.; Burazer, Lidija M.; Gavrović-Jankulović, Marija; Jankov, Ratko M.; Ćirković-Veličković, Tanja

(Blackwell Publishing, Oxford, 2008)

TY  - CONF
AU  - Polović, Natalija
AU  - Obradovic, A.
AU  - Spasic, M.
AU  - Plecas, B.
AU  - Burazer, Lidija M.
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/938
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - Transit times of kiwi fruit proteins through rat's gastrointestinal
VL  - 63
SP  - 428
EP  - 429
UR  - Kon_1891
ER  - 
@conference{
author = "Polović, Natalija and Obradovic, A. and Spasic, M. and Plecas, B. and Burazer, Lidija M. and Gavrović-Jankulović, Marija and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "Transit times of kiwi fruit proteins through rat's gastrointestinal",
volume = "63",
pages = "428-429",
url = "Kon_1891"
}
Polović, N., Obradovic, A., Spasic, M., Plecas, B., Burazer, L. M., Gavrović-Jankulović, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2008). Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy
Blackwell Publishing, Oxford., 63, 428-429.
Kon_1891
Polović N, Obradovic A, Spasic M, Plecas B, Burazer LM, Gavrović-Jankulović M, Jankov RM, Ćirković-Veličković T. Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy. 2008;63:428-429.
Kon_1891 .
Polović, Natalija, Obradovic, A., Spasic, M., Plecas, B., Burazer, Lidija M., Gavrović-Jankulović, Marija, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Transit times of kiwi fruit proteins through rat's gastrointestinal" in Allergy, 63 (2008):428-429,
Kon_1891 .