TY  - DATA
AU  - Dragačević, Luka
AU  - Lopandić, Zorana
AU  - Gavrović-Jankulović, Marija
AU  - Živković, Irena
AU  - Blagojević, Veljko
AU  - Polović, Natalija
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/642
AB  - SDS-PAGE showing: Lane 1 – purified banana lectin – BanLec; Lane 2 – chimera of banana lectin and enhanced green fluorescent protein BanLec-eGFP; Lane 3 – MW – molecular weight markers; Table 1. Repeatability of flow cytometric detection of different quantities of BL-eGFP binding to C. albicans; Table 2. Repeatability of ELLSA detection of different quantities of BanLec-B binding to C. albicans; Table 3. Repeatability of flow cytometric detection of different quantities of RCA120-FITC binding to L. casei DG; Table 4. Repeatability of ELLSA detection of different quantities of RCA120-B binding to L. casei DG; Table 5. Reproducibility of BanLec-B binding to 21 different microorganisms. Experiments were done in three different laboratories, with preparing new plates each time; Fig. 1 Determining linearity of ELLSA method, by measuring binding between C.albicans and different quantity of BanLec-B; Fig. 2 Determining linearity of flow cytometry, by measuring binding between C.albicans and different quantity of BanLec-eGFP; Fig. 3 Determining linearity of ELLSA method, by measuring binding between L.casei DG and different quantity of RCA120; Fig. 4 Determining linearity of flow cytometry, by measuring binding between L.casei DG and different quantity of RCA120.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Supplementary information for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.
EP  - 2060
SP  - 2047
VL  - 194
UR  - https://hdl.handle.net/21.15107/rcub_intor_642
ER  - 

@misc{
author = "Dragačević, Luka and Lopandić, Zorana and Gavrović-Jankulović, Marija and Živković, Irena and Blagojević, Veljko and Polović, Natalija and Minić, Rajna",
year = "2022",
abstract = "SDS-PAGE showing: Lane 1 – purified banana lectin – BanLec; Lane 2 – chimera of banana lectin and enhanced green fluorescent protein BanLec-eGFP; Lane 3 – MW – molecular weight markers; Table 1. Repeatability of flow cytometric detection of different quantities of BL-eGFP binding to C. albicans; Table 2. Repeatability of ELLSA detection of different quantities of BanLec-B binding to C. albicans; Table 3. Repeatability of flow cytometric detection of different quantities of RCA120-FITC binding to L. casei DG; Table 4. Repeatability of ELLSA detection of different quantities of RCA120-B binding to L. casei DG; Table 5. Reproducibility of BanLec-B binding to 21 different microorganisms. Experiments were done in three different laboratories, with preparing new plates each time; Fig. 1 Determining linearity of ELLSA method, by measuring binding between C.albicans and different quantity of BanLec-B; Fig. 2 Determining linearity of flow cytometry, by measuring binding between C.albicans and different quantity of BanLec-eGFP; Fig. 3 Determining linearity of ELLSA method, by measuring binding between L.casei DG and different quantity of RCA120; Fig. 4 Determining linearity of flow cytometry, by measuring binding between L.casei DG and different quantity of RCA120.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Supplementary information for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.",
pages = "2060-2047",
volume = "194",
url = "https://hdl.handle.net/21.15107/rcub_intor_642"
}

Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Supplementary information for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology
Springer., 194, 2047-2060.
https://hdl.handle.net/21.15107/rcub_intor_642

Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Supplementary information for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w.. in Applied Biochemistry and Biotechnology. 2022;194:2047-2060.
https://hdl.handle.net/21.15107/rcub_intor_642 .

Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Supplementary information for the article: Dragačević, L.; Lopandić, Z.; Gavrović-Jankulović, M.; Živković, I.; Blagojević, V.; Polović, N.; Minić, R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. Applied Biochemistry and Biotechnology 2022, 194, 2047–2060. https://doi.org/10.1007/s12010-021-03772-w." in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://hdl.handle.net/21.15107/rcub_intor_642 .

TY  - JOUR
AU  - Dragačević, Luka
AU  - Lopandić, Zorana
AU  - Gavrović-Jankulović, Marija
AU  - Živković, Irena
AU  - Blagojević, Veljko
AU  - Polović, Natalija
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/621
AB  - The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans
EP  - 2060
SP  - 2047
VL  - 194
DO  - 10.1007/s12010-021-03772-w
ER  - 

@article{
author = "Dragačević, Luka and Lopandić, Zorana and Gavrović-Jankulović, Marija and Živković, Irena and Blagojević, Veljko and Polović, Natalija and Minić, Rajna",
year = "2022",
abstract = "The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans",
pages = "2060-2047",
volume = "194",
doi = "10.1007/s12010-021-03772-w"
}

Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. in Applied Biochemistry and Biotechnology
Springer., 194, 2047-2060.
https://doi.org/10.1007/s12010-021-03772-w

Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. in Applied Biochemistry and Biotechnology. 2022;194:2047-2060.
doi:10.1007/s12010-021-03772-w .

Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans" in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://doi.org/10.1007/s12010-021-03772-w . .

TY  - JOUR
AU  - Malešević, Milka
AU  - Stanisavljević, Nemanja
AU  - Novović, Katarina
AU  - Polović, Natalija
AU  - Vasiljević, Zorica
AU  - Kojić, Milan
AU  - Jovčić, Branko
PY  - 2020
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1338
UR  - http://intor.torlakinstitut.com/handle/123456789/705
AB  - Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-DL-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Microbial Pathogenesis
T1  - Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity
VL  - 149
DO  - 10.1016/j.micpath.2020.104561
ER  - 

@article{
author = "Malešević, Milka and Stanisavljević, Nemanja and Novović, Katarina and Polović, Natalija and Vasiljević, Zorica and Kojić, Milan and Jovčić, Branko",
year = "2020",
abstract = "Burkholderia cepacia is well known as the causative agent of infections in humans where often shares niche with other pathogens, like Pseudomonas aeruginosa. Clinical isolate Burkholderia sp. BCC4135 was selected due to its strong quorum quenching (QQ) activity. Whole genome sequencing unveiled this isolate as B. cepacia with unique sequence type ST1485 and a myriad of genes belonging to resistome and virulome. Two QQ lactonases YtnP and Y2-aiiA originated from B. cepacia BCC4135 were cloned, expressed, and functionally characterized. They were active against a broad substrate spectrum of the N-acyl-homoserine lactones (AHLs). The YtnP lactonase was inactive, while Y2-aiiA was active against N-tetradecanoyl-DL-homoserine lactone (C14-HSL) which could imply the difference in their biological roles from the aspect of its quorum sensing (QS) autoregulation and interference with the QS systems of bacteria residing within the same niche. Both YtnP and Y2-aiiA were able to attenuate virulence potential of P. aeruginosa MMA83 clinical isolate declining its biofilm formation and virulence factors production. B. cepacia BCC4135 lactonases interfered with the las, rhl, and even pqs QS circuit of P. aeruginosa MMA83 transcription and the effect of combined enzymes was even more prominent. B. cepacia BCC4135 also employs the CepI/R QS system for governing its own virulence traits and possibly self-regulates the QQ/QS network through the different expression and activity of YtnP and/or Y2-aiiA. Our findings pointed out that BCC4135 lactonases could be exploited as an effective antivirulence drugs against P. aeruginosa and gave us a new insight into B. cepacia QQ/QS machinery.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Microbial Pathogenesis",
title = "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity",
volume = "149",
doi = "10.1016/j.micpath.2020.104561"
}

Malešević, M., Stanisavljević, N., Novović, K., Polović, N., Vasiljević, Z., Kojić, M.,& Jovčić, B.. (2020). Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis
Academic Press Ltd- Elsevier Science Ltd, London., 149.
https://doi.org/10.1016/j.micpath.2020.104561

Malešević M, Stanisavljević N, Novović K, Polović N, Vasiljević Z, Kojić M, Jovčić B. Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity. in Microbial Pathogenesis. 2020;149.
doi:10.1016/j.micpath.2020.104561 .

Malešević, Milka, Stanisavljević, Nemanja, Novović, Katarina, Polović, Natalija, Vasiljević, Zorica, Kojić, Milan, Jovčić, Branko, "Burkholderia cepacia YtnP and Y2-aiiA lactonases inhibit virulence of Pseudomonas aeruginosa via quorum quenching activity" in Microbial Pathogenesis, 149 (2020),
https://doi.org/10.1016/j.micpath.2020.104561 . .

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica
AU  - Polović, Natalija
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/358
AB  - Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Food and Chemical Toxicology
T1  - Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy
EP  - 1018
IS  - 3-4
SP  - 1013
VL  - 50
DO  - 10.1016/j.fct.2011.12.030
ER  - 

@article{
author = "Grozdanović, Milica and Popović, Milica and Polović, Natalija and Burazer, Lidija and Vučković, Olga and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Food and Chemical Toxicology",
title = "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy",
pages = "1018-1013",
number = "3-4",
volume = "50",
doi = "10.1016/j.fct.2011.12.030"
}

Grozdanović, M., Popović, M., Polović, N., Burazer, L., Vučković, O., Atanasković-Marković, M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2012). Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology
Pergamon-Elsevier Science Ltd, Oxford., 50(3-4), 1013-1018.
https://doi.org/10.1016/j.fct.2011.12.030

Grozdanović M, Popović M, Polović N, Burazer L, Vučković O, Atanasković-Marković M, Lindner B, Petersen A, Gavrović-Jankulović M. Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology. 2012;50(3-4):1013-1018.
doi:10.1016/j.fct.2011.12.030 .

Grozdanović, Milica, Popović, Milica, Polović, Natalija, Burazer, Lidija, Vučković, Olga, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy" in Food and Chemical Toxicology, 50, no. 3-4 (2012):1013-1018,
https://doi.org/10.1016/j.fct.2011.12.030 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Radosavljević, Jelena
AU  - Polović, Natalija
AU  - Jadranin, Milka
AU  - Popović, Milica
AU  - Vučković, Olga
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Veličković, Tanja
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/292
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 β-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.
T2  - International Dairy Journal
T1  - Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation
EP  - 752
IS  - 12
SP  - 746
VL  - 19
DO  - 10.1016/j.idairyj.2009.05.008
ER  - 

@article{
author = "Stanić, Dragana and Radosavljević, Jelena and Polović, Natalija and Jadranin, Milka and Popović, Milica and Vučković, Olga and Burazer, Lidija and Jankov, Ratko and 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 β-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.",
journal = "International Dairy Journal",
title = "Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation",
pages = "752-746",
number = "12",
volume = "19",
doi = "10.1016/j.idairyj.2009.05.008"
}

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

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

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

TY  - JOUR
AU  - Polović, Natalija
AU  - Pjanović, Rada V.
AU  - Burazer, Lidija
AU  - Velicković, Sava J.
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/269
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
EP  - 14
IS  - 1
SP  - 8
VL  - 89
DO  - 10.1002/jsfa.3404
ER  - 

@article{
author = "Polović, Natalija and Pjanović, Rada V. and Burazer, Lidija and Velicković, Sava J. and Jankov, Ratko 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",
pages = "14-8",
number = "1",
volume = "89",
doi = "10.1002/jsfa.3404"
}

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

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

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

TY  - CONF
AU  - Polović, Natalija
AU  - Obradović, A.
AU  - Spasić, M.
AU  - Plećaš, Bosiljka
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/253
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - Transit times of kiwi fruit proteins through rat's gastrointestinal
EP  - 429
SP  - 428
VL  - 63
UR  - https://hdl.handle.net/21.15107/rcub_intor_253
ER  - 

@conference{
author = "Polović, Natalija and Obradović, A. and Spasić, M. and Plećaš, Bosiljka and Burazer, Lidija and Gavrović-Jankulović, Marija and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "Transit times of kiwi fruit proteins through rat's gastrointestinal",
pages = "429-428",
volume = "63",
url = "https://hdl.handle.net/21.15107/rcub_intor_253"
}

Polović, N., Obradović, A., Spasić, M., Plećaš, B., Burazer, L., Gavrović-Jankulović, M., Jankov, R.,& Ćirković-Veličković, T.. (2008). Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy
Blackwell Publishing, Oxford., 63, 428-429.
https://hdl.handle.net/21.15107/rcub_intor_253

Polović N, Obradović A, Spasić M, Plećaš B, Burazer L, Gavrović-Jankulović M, Jankov R, Ćirković-Veličković T. Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy. 2008;63:428-429.
https://hdl.handle.net/21.15107/rcub_intor_253 .

Polović, Natalija, Obradović, A., Spasić, M., Plećaš, Bosiljka, Burazer, Lidija, Gavrović-Jankulović, Marija, Jankov, Ratko, Ćirković-Veličković, Tanja, "Transit times of kiwi fruit proteins through rat's gastrointestinal" in Allergy, 63 (2008):428-429,
https://hdl.handle.net/21.15107/rcub_intor_253 .

TY  - JOUR
AU  - Polović, Natalija
AU  - Blanuša, Milan
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Veličković, Tanja
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/225
AB  - Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
EP  - 771
IS  - 5
SP  - 764
VL  - 37
DO  - 10.1111/j.1365-2222.2007.02703.x
ER  - 

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

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

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

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

TY  - JOUR
AU  - Blanuša, Milan
AU  - Perović, Iva
AU  - Popović, Milica
AU  - Polović, Natalija
AU  - Burazer, Lidija
AU  - Milovanović, Mina
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/224
AB  - A simple ion-exchange HPLC-UV method was developed for determination of major allergens from mugwort pollen and kiwi fruit extracts in mass-units. The separation of Art v 1 and Act c 1 from other components in the extracts was achieved in one step. The extinction coefficients used in the study here theoretically determined and compared to the extinction coefficients determined by gravimetry. We also reported a close correlation of the major allergen contents with the overall allergenic potency of the extracts determined by inhibition ELISA. This method could be a useful tool for standardization of allergenic extracts for clinical use. (c) 2007 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences
T1  - Quantification of Art v 1 and Act c 1 being major allergens of mugwort pollen and kiwi fruit extracts in mass-units by ion-exchange HPLC-UV method
EP  - 194
IS  - 2
SP  - 188
VL  - 857
DO  - 10.1016/j.jchromb.2007.07.015
ER  - 

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

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

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

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

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Polović, Natalija
AU  - Gavrović-Jankulović, Marija
AU  - Burazer, Lidija
AU  - Đergović-Petrović, Danica
AU  - Vučković, Olga
AU  - Drobnjak, Olika
AU  - Šporčić, Zorica
AU  - Atanasković-Marković, Marina
AU  - Jankov, Ratko
PY  - 2006
UR  - http://intor.torlakinstitut.com/handle/123456789/220
AB  - Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones.
AB  - U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract
T1  - Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta
EP  - 888
IS  - 8-9
SP  - 879
VL  - 71
DO  - 10.2298/JSC0609879C
ER  - 

@article{
author = "Ćirković-Veličković, Tanja and Polović, Natalija and Gavrović-Jankulović, Marija and Burazer, Lidija and Đergović-Petrović, Danica and Vučković, Olga and Drobnjak, Olika and Šporčić, Zorica and Atanasković-Marković, Marina and Jankov, Ratko",
year = "2006",
abstract = "Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones., U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract, Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta",
pages = "888-879",
number = "8-9",
volume = "71",
doi = "10.2298/JSC0609879C"
}

Ćirković-Veličković, T., Polović, N., Gavrović-Jankulović, M., Burazer, L., Đergović-Petrović, D., Vučković, O., Drobnjak, O., Šporčić, Z., Atanasković-Marković, M.,& Jankov, R.. (2006). Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 71(8-9), 879-888.
https://doi.org/10.2298/JSC0609879C

Ćirković-Veličković T, Polović N, Gavrović-Jankulović M, Burazer L, Đergović-Petrović D, Vučković O, Drobnjak O, Šporčić Z, Atanasković-Marković M, Jankov R. Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society. 2006;71(8-9):879-888.
doi:10.2298/JSC0609879C .

Ćirković-Veličković, Tanja, Polović, Natalija, Gavrović-Jankulović, Marija, Burazer, Lidija, Đergović-Petrović, Danica, Vučković, Olga, Drobnjak, Olika, Šporčić, Zorica, Atanasković-Marković, Marina, Jankov, Ratko, "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract" in Journal of the Serbian Chemical Society, 71, no. 8-9 (2006):879-888,
https://doi.org/10.2298/JSC0609879C . .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
AU  - Prisić, S.
AU  - Jankov, Ratko
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
PY  - 2005
UR  - http://intor.torlakinstitut.com/handle/123456789/201
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
EP  - 128
IS  - 2
SP  - 117
VL  - 16
DO  - 10.1080/09540100500090804
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Polović, Natalija and Prisić, S. and Jankov, Ratko and Atanasković-Marković, Marina and Vučković, Olga 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",
pages = "128-117",
number = "2",
volume = "16",
doi = "10.1080/09540100500090804"
}

Gavrović-Jankulović, M., Polović, N., Prisić, S., Jankov, R., 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, Prisić S, Jankov R, 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, Prisić, S., Jankov, Ratko, Atanasković-Marković, Marina, Vučković, Olga, 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 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Burazer, Lidija
AU  - Đergović-Petrović, Danica
AU  - Vučković, Olga
AU  - Jankov, Ratko
PY  - 2004
UR  - http://intor.torlakinstitut.com/handle/123456789/184
AB  - This study considers the influence of exposure to simulated gastrointestinal conditions (saliva, gut, intestine and acidic conditions of the gut) on IgG binding of unmodified allergens and three types of LMW allergoids of Artemisia vulgaris pollen extract obtained by means of potassium cyanate succinic and maleic anhydride. It also concerns the optimization of a self-developed ELISA assay for comparison of the specific IgG binding of mugwort pollen extract and modified mugwort pollen derivatives. The ELISA was conducted with a mugwort pollen extract coupled to the plate, using the sera from 12 mugwort- pollen allergic patients. The exposure to saliva fluid for 2 min did not influence the IgG binding properties of allergens and allergoids. Exposure of mugwort pollen allergens and LMW allergoids to the acidic conditions of the gut did not dramatically change their IgG binding properties. By exposing mugwort pollen extract and LMW derivatives to the SGF conditions for 1 h, the percent of IgG binding epitopes was reduced to a half of its starting value in the extract and to about 30%in all the allergoid samples. After prolonged exposure only the carbamyl derivative showed reduced IgG binding. Changes of the IgG binding potential of all four samples after exposure in SIF followed a similar pattern.
AB  - Predmet ovog rada je ispitivanje promena IgG vezivanja nemodifikovanih alergena polena A. vulgaris i tri tipa alergoida malih molekulskih masa dobijenih tretmanom sa kalijum-cijanatom, i anhidridima ćilibarne i meleinske posle izlaganja uslovima gastrointestinalnog trakta (saliva, želudac, tanko crevo i kisela sredina želudačnog soka) i optimizacija domaćeg ELISA testa za određivanje IgG vezivanja alergena i alergoida polena pelina.UELISA testu je za pločicu kuplovan ekstrakt polena pelina i korišćeni su serumi 12 pacijenata alergičnih na pelin. Izlaganje salivi u trajanju od 2 minuta ne utiče na IgG vezujuće osobine alergena i alergoida. Izlaganje kiseloj sredini želudačnog soka značajno ne utiče na IgG vezujuće osobine alergena i alergoida polena pelina. Posle izlaganja simuliranom želudačnom soku alergena i derivata u trajanju od 1 sata, procenat IgG vezujućih epitopa u nemodifikovanom uzorku se smanjuje na polovinu početne vrednosti i na oko 30 % kod sva tri derivata. Jedino se kod karbamil-derivata % IgG vezivanja dodatno smanjuje sa produžavanjem izlaganja SGF-u.Promene u IgG vezujućem potencijalu sva 4 uzorka posle izlaganja simuliranim uslovima tankog creva prate sličan obrazac.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest
T1  - Igg vezivanje alergena i alergoida polena pelina prethodno izloženih simuliranim uslovima gastrointestinalnog trakta mereno domaćim elisa testom
EP  - 540
IS  - 7
SP  - 533
VL  - 69
DO  - 10.2298/JSC0407533P
ER  - 

@article{
author = "Polović, Natalija and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Burazer, Lidija and Đergović-Petrović, Danica and Vučković, Olga and Jankov, Ratko",
year = "2004",
abstract = "This study considers the influence of exposure to simulated gastrointestinal conditions (saliva, gut, intestine and acidic conditions of the gut) on IgG binding of unmodified allergens and three types of LMW allergoids of Artemisia vulgaris pollen extract obtained by means of potassium cyanate succinic and maleic anhydride. It also concerns the optimization of a self-developed ELISA assay for comparison of the specific IgG binding of mugwort pollen extract and modified mugwort pollen derivatives. The ELISA was conducted with a mugwort pollen extract coupled to the plate, using the sera from 12 mugwort- pollen allergic patients. The exposure to saliva fluid for 2 min did not influence the IgG binding properties of allergens and allergoids. Exposure of mugwort pollen allergens and LMW allergoids to the acidic conditions of the gut did not dramatically change their IgG binding properties. By exposing mugwort pollen extract and LMW derivatives to the SGF conditions for 1 h, the percent of IgG binding epitopes was reduced to a half of its starting value in the extract and to about 30%in all the allergoid samples. After prolonged exposure only the carbamyl derivative showed reduced IgG binding. Changes of the IgG binding potential of all four samples after exposure in SIF followed a similar pattern., Predmet ovog rada je ispitivanje promena IgG vezivanja nemodifikovanih alergena polena A. vulgaris i tri tipa alergoida malih molekulskih masa dobijenih tretmanom sa kalijum-cijanatom, i anhidridima ćilibarne i meleinske posle izlaganja uslovima gastrointestinalnog trakta (saliva, želudac, tanko crevo i kisela sredina želudačnog soka) i optimizacija domaćeg ELISA testa za određivanje IgG vezivanja alergena i alergoida polena pelina.UELISA testu je za pločicu kuplovan ekstrakt polena pelina i korišćeni su serumi 12 pacijenata alergičnih na pelin. Izlaganje salivi u trajanju od 2 minuta ne utiče na IgG vezujuće osobine alergena i alergoida. Izlaganje kiseloj sredini želudačnog soka značajno ne utiče na IgG vezujuće osobine alergena i alergoida polena pelina. Posle izlaganja simuliranom želudačnom soku alergena i derivata u trajanju od 1 sata, procenat IgG vezujućih epitopa u nemodifikovanom uzorku se smanjuje na polovinu početne vrednosti i na oko 30 % kod sva tri derivata. Jedino se kod karbamil-derivata % IgG vezivanja dodatno smanjuje sa produžavanjem izlaganja SGF-u.Promene u IgG vezujućem potencijalu sva 4 uzorka posle izlaganja simuliranim uslovima tankog creva prate sličan obrazac.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest, Igg vezivanje alergena i alergoida polena pelina prethodno izloženih simuliranim uslovima gastrointestinalnog trakta mereno domaćim elisa testom",
pages = "540-533",
number = "7",
volume = "69",
doi = "10.2298/JSC0407533P"
}

Polović, N., Ćirković-Veličković, T., Gavrović-Jankulović, M., Burazer, L., Đergović-Petrović, D., Vučković, O.,& Jankov, R.. (2004). IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 69(7), 533-540.
https://doi.org/10.2298/JSC0407533P

Polović N, Ćirković-Veličković T, Gavrović-Jankulović M, Burazer L, Đergović-Petrović D, Vučković O, Jankov R. IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest. in Journal of the Serbian Chemical Society. 2004;69(7):533-540.
doi:10.2298/JSC0407533P .

Polović, Natalija, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Burazer, Lidija, Đergović-Petrović, Danica, Vučković, Olga, Jankov, Ratko, "IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest" in Journal of the Serbian Chemical Society, 69, no. 7 (2004):533-540,
https://doi.org/10.2298/JSC0407533P . .