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  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/390
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
EP  - 105
IS  - 1
SP  - 100
VL  - 53
DO  - 10.1007/s12088-012-0319-2
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
pages = "105-100",
number = "1",
volume = "53",
doi = "10.1007/s12088-012-0319-2"
}

Popović, M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M.. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2

Popović M, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology. 2013;53(1):100-105.
doi:10.1007/s12088-012-0319-2 .

Popović, Milica, Anđelković, Uroš, Grozdanović, Milica, Aleksić, Ivana, Gavrović-Jankulović, Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" in Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Burazer, Lidija
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/350
AB  - For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pG EX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 con struct were employed for production of the protein induced by 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37°C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25°C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of a bout 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot an analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis.
AB  - Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli
T1  - Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli
EP  - 52
IS  - 1
SP  - 43
VL  - 77
DO  - 10.2298/JSC110309158A
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijević, Rajna and Burazer, Lidija and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pG EX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 con struct were employed for production of the protein induced by 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37°C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25°C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of a bout 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot an analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis., Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli, Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli",
pages = "52-43",
number = "1",
volume = "77",
doi = "10.2298/JSC110309158A"
}

Abughren, M., Popović, M., Dimitrijević, R., Burazer, L., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A

Abughren M, Popović M, Dimitrijević R, Burazer L, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society. 2012;77(1):43-52.
doi:10.2298/JSC110309158A .

Abughren, Mohamed, Popović, Milica, Dimitrijević, Rajna, Burazer, Lidija, Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli" in Journal of the Serbian Chemical Society, 77, no. 1 (2012):43-52,
https://doi.org/10.2298/JSC110309158A . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Burazer, Lidija
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/364
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Errata: Abughren, M.; Popović, M.; Dimitrijević, R.; Burazer, L.; Grozdanović, M.; Atanasković-Marković, M.; Gavrović-Jankulović, M. Optimization of the Heterologous Expression of Banana Glucanase in Escherichia Coli. Journal of the Serbian Chemical Society 2012, 77 (1), 43–52. https://doi.org/10.2298/JSC110309158A.
EP  - 258
IS  - 2
SP  - 257
VL  - 77
UR  - https://hdl.handle.net/21.15107/rcub_intor_364
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijević, Rajna and Burazer, Lidija and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Errata: Abughren, M.; Popović, M.; Dimitrijević, R.; Burazer, L.; Grozdanović, M.; Atanasković-Marković, M.; Gavrović-Jankulović, M. Optimization of the Heterologous Expression of Banana Glucanase in Escherichia Coli. Journal of the Serbian Chemical Society 2012, 77 (1), 43–52. https://doi.org/10.2298/JSC110309158A.",
pages = "258-257",
number = "2",
volume = "77",
url = "https://hdl.handle.net/21.15107/rcub_intor_364"
}

Abughren, M., Popović, M., Dimitrijević, R., Burazer, L., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Errata: Abughren, M.; Popović, M.; Dimitrijević, R.; Burazer, L.; Grozdanović, M.; Atanasković-Marković, M.; Gavrović-Jankulović, M. Optimization of the Heterologous Expression of Banana Glucanase in Escherichia Coli. Journal of the Serbian Chemical Society 2012, 77 (1), 43–52. https://doi.org/10.2298/JSC110309158A.. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 77(2), 257-258.
https://hdl.handle.net/21.15107/rcub_intor_364

Abughren M, Popović M, Dimitrijević R, Burazer L, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Errata: Abughren, M.; Popović, M.; Dimitrijević, R.; Burazer, L.; Grozdanović, M.; Atanasković-Marković, M.; Gavrović-Jankulović, M. Optimization of the Heterologous Expression of Banana Glucanase in Escherichia Coli. Journal of the Serbian Chemical Society 2012, 77 (1), 43–52. https://doi.org/10.2298/JSC110309158A.. in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
https://hdl.handle.net/21.15107/rcub_intor_364 .

Abughren, Mohamed, Popović, Milica, Dimitrijević, Rajna, Burazer, Lidija, Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Errata: Abughren, M.; Popović, M.; Dimitrijević, R.; Burazer, L.; Grozdanović, M.; Atanasković-Marković, M.; Gavrović-Jankulović, M. Optimization of the Heterologous Expression of Banana Glucanase in Escherichia Coli. Journal of the Serbian Chemical Society 2012, 77 (1), 43–52. https://doi.org/10.2298/JSC110309158A." in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
https://hdl.handle.net/21.15107/rcub_intor_364 .

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  - CONF
AU  - Popović, Milica
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/316
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed
EP  - 323
SP  - 323
VL  - 65
UR  - https://hdl.handle.net/21.15107/rcub_intor_316
ER  - 

@conference{
author = "Popović, Milica and Burazer, Lidija and Vučković, Olga and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2010",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed",
pages = "323-323",
volume = "65",
url = "https://hdl.handle.net/21.15107/rcub_intor_316"
}

Popović, M., Burazer, L., Vučković, O., Jankov, R.,& Gavrović-Jankulović, M.. (2010). Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed. in Allergy
Wiley-Blackwell, Hoboken., 65, 323-323.
https://hdl.handle.net/21.15107/rcub_intor_316

Popović M, Burazer L, Vučković O, Jankov R, Gavrović-Jankulović M. Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed. in Allergy. 2010;65:323-323.
https://hdl.handle.net/21.15107/rcub_intor_316 .

Popović, Milica, Burazer, Lidija, Vučković, Olga, Jankov, Ratko, Gavrović-Jankulović, Marija, "Evaluation of allergenic properties of cysteine protease inhibitor from common ragweed" in Allergy, 65 (2010):323-323,
https://hdl.handle.net/21.15107/rcub_intor_316 .

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  - 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  - 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  - 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 . .