Prisic, S

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orcid::0000-0003-3137-4358
  • Prisic, S (3)
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Author's Bibliography

Allergenic potency of kiwi fruit during fruit development

Gavrović-Jankulović, Marija; Polović, Natalija; Prisic, S; Jankov, Ratko M.; Atanasković-Marković, Marina; Vučković, O.; Ćirković-Veličković, Tanja

(Taylor & Francis Ltd, Abingdon, 2005)

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
AU  - Prisic, S
AU  - Jankov, Ratko M.
AU  - Atanasković-Marković, Marina
AU  - Vučković, O.
AU  - Ćirković-Veličković, Tanja
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/711
AB  - Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Food and Agricultural Immunology
T1  - Allergenic potency of kiwi fruit during fruit development
VL  - 16
IS  - 2
SP  - 117
EP  - 128
DO  - 10.1080/09540100500090804
ER  - 
@article{
author = "Gavrović-Jankulović, Marija and Polović, Natalija and Prisic, S and Jankov, Ratko M. and Atanasković-Marković, Marina and Vučković, O. and Ćirković-Veličković, Tanja",
year = "2005",
abstract = "Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Food and Agricultural Immunology",
title = "Allergenic potency of kiwi fruit during fruit development",
volume = "16",
number = "2",
pages = "117-128",
doi = "10.1080/09540100500090804"
}
Gavrović-Jankulović, M., Polović, N., Prisic, S., Jankov, R. M., Atanasković-Marković, M., Vučković, O.,& Ćirković-Veličković, T.. (2005). Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology
Taylor & Francis Ltd, Abingdon., 16(2), 117-128.
https://doi.org/10.1080/09540100500090804
Gavrović-Jankulović M, Polović N, Prisic S, Jankov RM, Atanasković-Marković M, Vučković O, Ćirković-Veličković T. Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology. 2005;16(2):117-128.
doi:10.1080/09540100500090804 .
Gavrović-Jankulović, Marija, Polović, Natalija, Prisic, S, Jankov, Ratko M., Atanasković-Marković, Marina, Vučković, O., Ćirković-Veličković, Tanja, "Allergenic potency of kiwi fruit during fruit development" in Food and Agricultural Immunology, 16, no. 2 (2005):117-128,
https://doi.org/10.1080/09540100500090804 . .
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Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis

Nedić, Olgica; Nikolić, J. A.; Prisic, S; Aćimović, Jelena M.; Hajdukovic-Dragojlovic, L

(Carfax Publishing, Basingstoke, 2003)

TY  - JOUR
AU  - Nedić, Olgica
AU  - Nikolić, J. A.
AU  - Prisic, S
AU  - Aćimović, Jelena M.
AU  - Hajdukovic-Dragojlovic, L
PY  - 2003
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/543
AB  - The capacity of the liver to synthesize insulin-like growth factors (IGFs) and their binding proteins (IGFBPs) may be compromised by alcohol. The characteristics of IGFBP-3 variants obtained from healthy individuals and patients with alcoholic cirrhosis (ALC) were compared. Concanavalin A (Con A) affinity electrophoresis and ligand blotting demonstrated that there was a gradual change in carbohydrate properties of putative IGFBP-3 with progression of ALC from stages A to C. As many as 12 ionic species of IGFBP-3 could be distinguished, corresponding probably to variously glycosylated and/or phosphorylated isoforms of the core protein. Three of them reacted significantly with the immobilized Con A, the pattern being altered in patients with ALC. Patients with ALC in stage B exhibited the presence of clearly differentiated IGFBP-3 variants less and more Con A reactive, suggesting this stage to be a turning point with the most intensive changes in the IGF-IGFBP system. Because the glycosylation pattern is tissue specific, pathological post-translational modifications found for one glycoprotein (IGFBP-3) are probably shared by others of the same tissue origin. This may affect their susceptibility to proteolysis and subsequently their function.
PB  - Carfax Publishing, Basingstoke
T2  - Addiction Biology
T1  - Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis
VL  - 8
IS  - 1
SP  - 81
EP  - 88
DO  - 10.1080/1355621031000069927
ER  - 
@article{
author = "Nedić, Olgica and Nikolić, J. A. and Prisic, S and Aćimović, Jelena M. and Hajdukovic-Dragojlovic, L",
year = "2003",
abstract = "The capacity of the liver to synthesize insulin-like growth factors (IGFs) and their binding proteins (IGFBPs) may be compromised by alcohol. The characteristics of IGFBP-3 variants obtained from healthy individuals and patients with alcoholic cirrhosis (ALC) were compared. Concanavalin A (Con A) affinity electrophoresis and ligand blotting demonstrated that there was a gradual change in carbohydrate properties of putative IGFBP-3 with progression of ALC from stages A to C. As many as 12 ionic species of IGFBP-3 could be distinguished, corresponding probably to variously glycosylated and/or phosphorylated isoforms of the core protein. Three of them reacted significantly with the immobilized Con A, the pattern being altered in patients with ALC. Patients with ALC in stage B exhibited the presence of clearly differentiated IGFBP-3 variants less and more Con A reactive, suggesting this stage to be a turning point with the most intensive changes in the IGF-IGFBP system. Because the glycosylation pattern is tissue specific, pathological post-translational modifications found for one glycoprotein (IGFBP-3) are probably shared by others of the same tissue origin. This may affect their susceptibility to proteolysis and subsequently their function.",
publisher = "Carfax Publishing, Basingstoke",
journal = "Addiction Biology",
title = "Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis",
volume = "8",
number = "1",
pages = "81-88",
doi = "10.1080/1355621031000069927"
}
Nedić, O., Nikolić, J. A., Prisic, S., Aćimović, J. M.,& Hajdukovic-Dragojlovic, L.. (2003). Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis. in Addiction Biology
Carfax Publishing, Basingstoke., 8(1), 81-88.
https://doi.org/10.1080/1355621031000069927
Nedić O, Nikolić JA, Prisic S, Aćimović JM, Hajdukovic-Dragojlovic L. Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis. in Addiction Biology. 2003;8(1):81-88.
doi:10.1080/1355621031000069927 .
Nedić, Olgica, Nikolić, J. A., Prisic, S, Aćimović, Jelena M., Hajdukovic-Dragojlovic, L, "Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis" in Addiction Biology, 8, no. 1 (2003):81-88,
https://doi.org/10.1080/1355621031000069927 . .
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The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties

Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija; Prisic, S; Jankov, Ratko M.; Burazer, Lidija M.; Vučković, O.; Sporcic, Z; Paranos, S

(Blackwell Munksgaard, Copenhagen, 2002)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Prisic, S
AU  - Jankov, Ratko M.
AU  - Burazer, Lidija M.
AU  - Vučković, O.
AU  - Sporcic, Z
AU  - Paranos, S
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/509
AB  - Background: Reaction of epsilon-amino groups of lysine with potassium cyanate, maleic, or succinic anhydride leads to allergoids of low molecular weight. No study has been performed to compare their properties and investigate the influence of a residual group on allergenicity and human IgE- and IgG-binding of these derivatives. Methods: Allergoids of a pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, and succinic and maleic anhydride. Biochemical properties were investigated by determination of amino groups, enzyme activity, isoelectric focusing IEF and SDS-PAGE. IgE- and IgG-binding was determined using immunoblots and ELISA inhibition. Allergenicity was investigated by skin prick tests (SPT) on a group of 52 patients, of which 6 were control subjects, 30 were patients with no previous immunotherapy (IT), and 16 were patients undergoing immunotherapy. Results: The same degree of amino-group modification (more than 85%), residual enzyme activity (less then 15%), IEF, and SDS-PAGE pattern were noted. In the immunoblots of IgE-binding, there was more pronounced reduction in the succinyl and maleyl derivatives than in the carbamyl one. IgG-binding was less affected by carbamylation than by acid anhydride modification. The SPT showed that the succinylated derivative had the most reduced allergenicity (98% showed a reduced wheal diameter when tested with the succinyl derivative, 87% with the maleyl allergoid, and 83% with the carbamyl allergoid). The most significant difference among allergoids could be seen in the group of patients with high skin reactivity (83% of patients showed no reaction to the succinyl derivative when compared to the value of 28% for the carbamyl derivative or 22% for the maleyl derivative). Conclusions: According to our results, all three modification procedures yielded allergoids with a similar extent of modification. No single biochemical parameter investigated in the study could predict the degree of reduced allergenicity in vivo. The most reduced allergenicity was seen in the succinyl derivative while the preservation of IgG binding epitopes was of the highest degree for the carbamyl derivative.
PB  - Blackwell Munksgaard, Copenhagen
T2  - Allergy
T1  - The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties
VL  - 57
IS  - 11
SP  - 1013
EP  - 1020
DO  - 10.1034/j.1398-9995.2002.23739.x
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Prisic, S and Jankov, Ratko M. and Burazer, Lidija M. and Vučković, O. and Sporcic, Z and Paranos, S",
year = "2002",
abstract = "Background: Reaction of epsilon-amino groups of lysine with potassium cyanate, maleic, or succinic anhydride leads to allergoids of low molecular weight. No study has been performed to compare their properties and investigate the influence of a residual group on allergenicity and human IgE- and IgG-binding of these derivatives. Methods: Allergoids of a pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, and succinic and maleic anhydride. Biochemical properties were investigated by determination of amino groups, enzyme activity, isoelectric focusing IEF and SDS-PAGE. IgE- and IgG-binding was determined using immunoblots and ELISA inhibition. Allergenicity was investigated by skin prick tests (SPT) on a group of 52 patients, of which 6 were control subjects, 30 were patients with no previous immunotherapy (IT), and 16 were patients undergoing immunotherapy. Results: The same degree of amino-group modification (more than 85%), residual enzyme activity (less then 15%), IEF, and SDS-PAGE pattern were noted. In the immunoblots of IgE-binding, there was more pronounced reduction in the succinyl and maleyl derivatives than in the carbamyl one. IgG-binding was less affected by carbamylation than by acid anhydride modification. The SPT showed that the succinylated derivative had the most reduced allergenicity (98% showed a reduced wheal diameter when tested with the succinyl derivative, 87% with the maleyl allergoid, and 83% with the carbamyl allergoid). The most significant difference among allergoids could be seen in the group of patients with high skin reactivity (83% of patients showed no reaction to the succinyl derivative when compared to the value of 28% for the carbamyl derivative or 22% for the maleyl derivative). Conclusions: According to our results, all three modification procedures yielded allergoids with a similar extent of modification. No single biochemical parameter investigated in the study could predict the degree of reduced allergenicity in vivo. The most reduced allergenicity was seen in the succinyl derivative while the preservation of IgG binding epitopes was of the highest degree for the carbamyl derivative.",
publisher = "Blackwell Munksgaard, Copenhagen",
journal = "Allergy",
title = "The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties",
volume = "57",
number = "11",
pages = "1013-1020",
doi = "10.1034/j.1398-9995.2002.23739.x"
}
Ćirković-Veličković, T., Gavrović-Jankulović, M., Prisic, S., Jankov, R. M., Burazer, L. M., Vučković, O., Sporcic, Z.,& Paranos, S.. (2002). The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties. in Allergy
Blackwell Munksgaard, Copenhagen., 57(11), 1013-1020.
https://doi.org/10.1034/j.1398-9995.2002.23739.x
Ćirković-Veličković T, Gavrović-Jankulović M, Prisic S, Jankov RM, Burazer LM, Vučković O, Sporcic Z, Paranos S. The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties. in Allergy. 2002;57(11):1013-1020.
doi:10.1034/j.1398-9995.2002.23739.x .
Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Prisic, S, Jankov, Ratko M., Burazer, Lidija M., Vučković, O., Sporcic, Z, Paranos, S, "The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties" in Allergy, 57, no. 11 (2002):1013-1020,
https://doi.org/10.1034/j.1398-9995.2002.23739.x . .
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