TY  - JOUR
AU  - Grozdanović, Milica
AU  - Ostojić, Sanja
AU  - Aleksić, Ivana
AU  - Anđelković, Uroš
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/411
AB  - BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
EP  - 3052
IS  - 14
SP  - 3046
VL  - 94
DO  - 10.1002/jsfa.6656
ER  - 

@article{
author = "Grozdanović, Milica and Ostojić, Sanja and Aleksić, Ivana and Anđelković, Uroš and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart",
pages = "3052-3046",
number = "14",
volume = "94",
doi = "10.1002/jsfa.6656"
}

Grozdanović, M., Ostojić, S., Aleksić, I., Anđelković, U., Petersen, A.,& Gavrović-Jankulović, M.. (2014). Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 94(14), 3046-3052.
https://doi.org/10.1002/jsfa.6656

Grozdanović M, Ostojić S, Aleksić I, Anđelković U, Petersen A, Gavrović-Jankulović M. Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture. 2014;94(14):3046-3052.
doi:10.1002/jsfa.6656 .

Grozdanović, Milica, Ostojić, Sanja, Aleksić, Ivana, Anđelković, Uroš, Petersen, Arnd, Gavrović-Jankulović, Marija, "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart" in Journal of the Science of Food and Agriculture, 94, no. 14 (2014):3046-3052,
https://doi.org/10.1002/jsfa.6656 . .

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/388
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.
PB  - Elsevier Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
EP  - 59
SP  - 53
VL  - 94
DO  - 10.1016/j.phytochem.2013.06.006
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.",
publisher = "Elsevier Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
pages = "59-53",
volume = "94",
doi = "10.1016/j.phytochem.2013.06.006"
}

Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Elsevier Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006

Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006 .

Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 . .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/362
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
EP  - 453
IS  - 3
SP  - 446
VL  - 56
DO  - 10.1002/mnfr.201100541
ER  - 

@article{
author = "Aleksić, Ivana and Popović, Milica and Dimitrijević, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
pages = "453-446",
number = "3",
volume = "56",
doi = "10.1002/mnfr.201100541"
}

Aleksić, I., Popović, M., Dimitrijević, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research
Wiley, Hoboken., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541

Aleksić I, Popović M, Dimitrijević R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .

Aleksić, Ivana, Popović, Milica, Dimitrijević, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition and Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .

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  - Popović, Milica
AU  - Milovanović, Mina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Hoffmann-Sommergruber, Karin
AU  - Knulst, Andre C.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/305
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, Hoboken
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
EP  - 380
IS  - 3
SP  - 373
VL  - 54
DO  - 10.1002/mnfr.200900035
ER  - 

@article{
author = "Popović, Milica and Milovanović, Mina and Burazer, Lidija and Vučković, Olga and Hoffmann-Sommergruber, Karin and Knulst, Andre C. and Lindner, Buko and Petersen, Arnd and Jankov, Ratko 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, Hoboken",
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",
pages = "380-373",
number = "3",
volume = "54",
doi = "10.1002/mnfr.200900035"
}

Popović, M., Milovanović, M., Burazer, L., Vučković, O., Hoffmann-Sommergruber, K., Knulst, A. C., Lindner, B., Petersen, A., Jankov, R.,& 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, Hoboken., 54(3), 373-380.
https://doi.org/10.1002/mnfr.200900035

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

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

TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Dimitrijević, Ljiljana
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/275
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, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
EP  - 2115
IS  - 6
SP  - 2108
VL  - 107
DO  - 10.1111/j.1365-2672.2009.04539.x
ER  - 

@article{
author = "Dimitrijević, Rajna and Stojanović, Marijana and Živković, Irena and Petersen, Arnd and Jankov, Ratko and Dimitrijević, Ljiljana 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, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
pages = "2115-2108",
number = "6",
volume = "107",
doi = "10.1111/j.1365-2672.2009.04539.x"
}

Dimitrijević, R., Stojanović, M., Živković, I., Petersen, A., Jankov, R., Dimitrijević, 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, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x

Dimitrijević R, Stojanović M, Živković I, Petersen A, Jankov R, Dimitrijević 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 .

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

TY  - CONF
AU  - Popović, Milica
AU  - Milovanović, Mina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Knulst, Andre C.
AU  - Hoffmann-Sommergruber, Karin
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/276
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy
EP  - 271
SP  - 270
VL  - 64
UR  - https://hdl.handle.net/21.15107/rcub_intor_276
ER  - 

@conference{
author = "Popović, Milica and Milovanović, Mina and Burazer, Lidija and Vučković, Olga and Knulst, Andre C. and Hoffmann-Sommergruber, Karin and Lindner, Buko and Petersen, Arnd and Jankov, Ratko 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",
pages = "271-270",
volume = "64",
url = "https://hdl.handle.net/21.15107/rcub_intor_276"
}

Popović, M., Milovanović, M., Burazer, L., Vučković, O., Knulst, A. C., Hoffmann-Sommergruber, K., Lindner, B., Petersen, A., Jankov, R.,& 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.
https://hdl.handle.net/21.15107/rcub_intor_276

Popović M, Milovanović M, Burazer L, Vučković O, Knulst AC, Hoffmann-Sommergruber K, Lindner B, Petersen A, Jankov R, Gavrović-Jankulović M. Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Allergy. 2009;64:270-271.
https://hdl.handle.net/21.15107/rcub_intor_276 .

Popović, Milica, Milovanović, Mina, Burazer, Lidija, Vučković, Olga, Knulst, Andre C., Hoffmann-Sommergruber, Karin, Lindner, Buko, Petersen, Arnd, Jankov, Ratko, Gavrović-Jankulović, Marija, "Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy" in Allergy, 64 (2009):270-271,
https://hdl.handle.net/21.15107/rcub_intor_276 .

TY  - CONF
AU  - Milovanović, Mina
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Becker, Wolf-Meinhard
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/271
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy
EP  - 80
SP  - 80
VL  - 64
UR  - https://hdl.handle.net/21.15107/rcub_intor_271
ER  - 

@conference{
author = "Milovanović, Mina and Atanasković-Marković, Marina and Vučković, Olga and Becker, Wolf-Meinhard and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy",
pages = "80-80",
volume = "64",
url = "https://hdl.handle.net/21.15107/rcub_intor_271"
}

Milovanović, M., Atanasković-Marković, M., Vučković, O., Becker, W., Petersen, A.,& Gavrović-Jankulović, M.. (2009). Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 80-80.
https://hdl.handle.net/21.15107/rcub_intor_271

Milovanović M, Atanasković-Marković M, Vučković O, Becker W, Petersen A, Gavrović-Jankulović M. Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy. in Allergy. 2009;64:80-80.
https://hdl.handle.net/21.15107/rcub_intor_271 .

Milovanović, Mina, Atanasković-Marković, Marina, Vučković, Olga, Becker, Wolf-Meinhard, Petersen, Arnd, Gavrović-Jankulović, Marija, "Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy" in Allergy, 64 (2009):80-80,
https://hdl.handle.net/21.15107/rcub_intor_271 .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Spasic, Milena
AU  - Veličković, Tanja
AU  - Stojanović, Marijana
AU  - Inić-Kanada, Aleksandra
AU  - Dimitrijevic, Ljiliana
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Becker, Wolf-Meinhard
AU  - Jankov, Ratko
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/248
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 kiwifruit-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.
T2  - Molecular Nutrition and Food Research
T1  - Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA
EP  - 707
IS  - 6
SP  - 701
VL  - 52
DO  - 10.1002/mnfr.200700286
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Spasic, Milena and Veličković, Tanja and Stojanović, Marijana and Inić-Kanada, Aleksandra and Dimitrijevic, Ljiliana and Lindner, Buko and Petersen, Arnd and Becker, Wolf-Meinhard and Jankov, Ratko",
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 kiwifruit-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.",
journal = "Molecular Nutrition and Food Research",
title = "Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA",
pages = "707-701",
number = "6",
volume = "52",
doi = "10.1002/mnfr.200700286"
}

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

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

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

TY  - CONF
AU  - Popović, Milica
AU  - Burazer, Lidija
AU  - Atanasković-Marković, Marina
AU  - Milovanović, Mina
AU  - Ćirković-Veličković, Tanja
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Becker, Wolf-Meinhard
AU  - Gavrović-Jankulović, Marija
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/255
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
EP  - 573
SP  - 573
VL  - 63
UR  - https://hdl.handle.net/21.15107/rcub_intor_255
ER  - 

@conference{
author = "Popović, Milica and Burazer, Lidija and Atanasković-Marković, Marina and Milovanović, Mina and Ćirković-Veličković, Tanja and Petersen, Arnd and Jankov, Ratko and Becker, Wolf-Meinhard 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",
pages = "573-573",
volume = "63",
url = "https://hdl.handle.net/21.15107/rcub_intor_255"
}

Popović, M., Burazer, L., Atanasković-Marković, M., Milovanović, M., Ćirković-Veličković, T., Petersen, A., Jankov, R., 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.
https://hdl.handle.net/21.15107/rcub_intor_255

Popović M, Burazer L, Atanasković-Marković M, Milovanović M, Ćirković-Veličković T, Petersen A, Jankov R, 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.
https://hdl.handle.net/21.15107/rcub_intor_255 .

Popović, Milica, Burazer, Lidija, Atanasković-Marković, Marina, Milovanović, Mina, Ćirković-Veličković, Tanja, Petersen, Arnd, Jankov, Ratko, Becker, Wolf-Meinhard, 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,
https://hdl.handle.net/21.15107/rcub_intor_255 .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković, Tanja
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Petersen, Arnd
AU  - Gojgić, G.
AU  - Burazer, Lidija
AU  - Jankov, Ratko
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/150
AB  - Background: Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30-kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS). Objective: The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically. Methods: Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A-binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically. Results: All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A-binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE inummoblot. The TLP elicited positive skin prick test responses in 4 (80%) of 5 patients with OAS. Conclusion: This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.
PB  - Mosby-Elsevier, New York
T2  - Journal of Allergy and Clinical Immunology
T1  - Isolation and biochemical characterization of a thaumatin-like kiwi allergen
EP  - 810
IS  - 5
SP  - 805
VL  - 110
DO  - 10.1067/mai.2002.128947
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Ćirković, Tanja and Vučković, Olga and Atanasković-Marković, Marina and Petersen, Arnd and Gojgić, G. and Burazer, Lidija and Jankov, Ratko",
year = "2002",
abstract = "Background: Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30-kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS). Objective: The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically. Methods: Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A-binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically. Results: All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A-binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE inummoblot. The TLP elicited positive skin prick test responses in 4 (80%) of 5 patients with OAS. Conclusion: This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.",
publisher = "Mosby-Elsevier, New York",
journal = "Journal of Allergy and Clinical Immunology",
title = "Isolation and biochemical characterization of a thaumatin-like kiwi allergen",
pages = "810-805",
number = "5",
volume = "110",
doi = "10.1067/mai.2002.128947"
}

Gavrović-Jankulović, M., Ćirković, T., Vučković, O., Atanasković-Marković, M., Petersen, A., Gojgić, G., Burazer, L.,& Jankov, R.. (2002). Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology
Mosby-Elsevier, New York., 110(5), 805-810.
https://doi.org/10.1067/mai.2002.128947

Gavrović-Jankulović M, Ćirković T, Vučković O, Atanasković-Marković M, Petersen A, Gojgić G, Burazer L, Jankov R. Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology. 2002;110(5):805-810.
doi:10.1067/mai.2002.128947 .

Gavrović-Jankulović, Marija, Ćirković, Tanja, Vučković, Olga, Atanasković-Marković, Marina, Petersen, Arnd, Gojgić, G., Burazer, Lidija, Jankov, Ratko, "Isolation and biochemical characterization of a thaumatin-like kiwi allergen" in Journal of Allergy and Clinical Immunology, 110, no. 5 (2002):805-810,
https://doi.org/10.1067/mai.2002.128947 . .

TY  - CONF
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko
AU  - Petersen, Arnd
AU  - Vučković, Olga
AU  - Burazer, Lidija
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/148
PB  - Wiley, Hoboken
C3  - Allergy
T1  - Biochemical characterization of thaumatin-like kiwi allergen
EP  - 285
SP  - 285
VL  - 57
UR  - https://hdl.handle.net/21.15107/rcub_intor_148
ER  - 

@conference{
author = "Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Jankov, Ratko and Petersen, Arnd and Vučković, Olga and Burazer, Lidija",
year = "2002",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "Biochemical characterization of thaumatin-like kiwi allergen",
pages = "285-285",
volume = "57",
url = "https://hdl.handle.net/21.15107/rcub_intor_148"
}

Gavrović-Jankulović, M., Ćirković-Veličković, T., Jankov, R., Petersen, A., Vučković, O.,& Burazer, L.. (2002). Biochemical characterization of thaumatin-like kiwi allergen. in Allergy
Wiley, Hoboken., 57, 285-285.
https://hdl.handle.net/21.15107/rcub_intor_148

Gavrović-Jankulović M, Ćirković-Veličković T, Jankov R, Petersen A, Vučković O, Burazer L. Biochemical characterization of thaumatin-like kiwi allergen. in Allergy. 2002;57:285-285.
https://hdl.handle.net/21.15107/rcub_intor_148 .

Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Jankov, Ratko, Petersen, Arnd, Vučković, Olga, Burazer, Lidija, "Biochemical characterization of thaumatin-like kiwi allergen" in Allergy, 57 (2002):285-285,
https://hdl.handle.net/21.15107/rcub_intor_148 .