TY  - JOUR
AU  - Nikolić, Jasna
AU  - Mrkić, Ivan
AU  - Grozdanović, Milica
AU  - Popović, Milica M.
AU  - Petersen, Arnd
AU  - Jappe, Uta
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1804
AB  - Banana fruit (Musa acuminata) has become an important food allergen source in recent years. So far, 5 IgE reactive banana proteins have been identified, and the major allergens are: Mus a 2 (a class I chitinase, 31 kDa),Mus a4 (thaumatin-like protein, 21 kDa), and Mus a 5 (beta-1,3-glucanase,33 kDa). Due to variations in allergen expression levels, diagnostic reagents for food allergy can be improved by using individual allergen components instead of banana allergen extracts. The purpose of this study was to optimize the purification protocol of the three major allergens present in banana fruit: Mus a 2, Mus a 4 and Mus a 5. By employing a three-step purification protocol (a combination of anion-exchange, cation-exchange and reversed-phase chromatography) three important banana allergens were obtained in sufficient yield and high purity. Characterization of the purified proteins was performed by both biochemical (2-D PAGE, mass fingerprint and N-terminal sequencing) and immunochemical (immunoblot) methods. IgE reactivity to the purified allergens was tested by employing sera of five allergic patients. The purified allergens displayed higher sensitivity in IgE detection than the routinely used extracts. The three purified allergens are good candidates for reagents in component-based diagnosis of banana allergy. (C) 2014 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Chromatography B: Analytical Technologies in the Biomedical and L
T1  - Protocol for simultaneous isolation of three important banana allergens
VL  - 962
SP  - 30
EP  - 36
DO  - 10.1016/j.jchromb.2014.05.020
ER  - 

@article{
author = "Nikolić, Jasna and Mrkić, Ivan and Grozdanović, Milica and Popović, Milica M. and Petersen, Arnd and Jappe, Uta and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "Banana fruit (Musa acuminata) has become an important food allergen source in recent years. So far, 5 IgE reactive banana proteins have been identified, and the major allergens are: Mus a 2 (a class I chitinase, 31 kDa),Mus a4 (thaumatin-like protein, 21 kDa), and Mus a 5 (beta-1,3-glucanase,33 kDa). Due to variations in allergen expression levels, diagnostic reagents for food allergy can be improved by using individual allergen components instead of banana allergen extracts. The purpose of this study was to optimize the purification protocol of the three major allergens present in banana fruit: Mus a 2, Mus a 4 and Mus a 5. By employing a three-step purification protocol (a combination of anion-exchange, cation-exchange and reversed-phase chromatography) three important banana allergens were obtained in sufficient yield and high purity. Characterization of the purified proteins was performed by both biochemical (2-D PAGE, mass fingerprint and N-terminal sequencing) and immunochemical (immunoblot) methods. IgE reactivity to the purified allergens was tested by employing sera of five allergic patients. The purified allergens displayed higher sensitivity in IgE detection than the routinely used extracts. The three purified allergens are good candidates for reagents in component-based diagnosis of banana allergy. (C) 2014 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Chromatography B: Analytical Technologies in the Biomedical and L",
title = "Protocol for simultaneous isolation of three important banana allergens",
volume = "962",
pages = "30-36",
doi = "10.1016/j.jchromb.2014.05.020"
}

Nikolić, J., Mrkić, I., Grozdanović, M., Popović, M. M., Petersen, A., Jappe, U.,& Gavrović-Jankulović, M.. (2014). Protocol for simultaneous isolation of three important banana allergens. in Journal of Chromatography B: Analytical Technologies in the Biomedical and L
Elsevier Science Bv, Amsterdam., 962, 30-36.
https://doi.org/10.1016/j.jchromb.2014.05.020

Nikolić J, Mrkić I, Grozdanović M, Popović MM, Petersen A, Jappe U, Gavrović-Jankulović M. Protocol for simultaneous isolation of three important banana allergens. in Journal of Chromatography B: Analytical Technologies in the Biomedical and L. 2014;962:30-36.
doi:10.1016/j.jchromb.2014.05.020 .

Nikolić, Jasna, Mrkić, Ivan, Grozdanović, Milica, Popović, Milica M., Petersen, Arnd, Jappe, Uta, Gavrović-Jankulović, Marija, "Protocol for simultaneous isolation of three important banana allergens" in Journal of Chromatography B: Analytical Technologies in the Biomedical and L, 962 (2014):30-36,
https://doi.org/10.1016/j.jchromb.2014.05.020 . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1612
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)
VL  - 53
IS  - 1
SP  - 100
EP  - 105
DO  - 10.1007/s12088-012-0319-2
ER  - 

@article{
author = "Popović, Milica M. 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)",
volume = "53",
number = "1",
pages = "100-105",
doi = "10.1007/s12088-012-0319-2"
}

Popović, M. 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 MM, 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 M., 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  - Popović, Milica M.
AU  - Grozdanović, Milica
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1623
AB  - Since its first appearance on the market, kiwifruit has become very popular in the human diet due to its pleasant taste, low caloric value and high content of vitamin C. However, kiwifruit allergy has become a frequent cause of type I hypersensitivity in the western society. The molecular basis for kiwifruit allergy has been ascribed to up-to-now 11 identified IgE reactive molecules. They are proteins and glycoproteins with a molecular mass between 10 and 50 kDa. The major kiwifruit allergen is a cysteine protease denoted as Act d 1, which represents 50 % of the soluble protein extract. Due to differences in the abundance of the protein components and biological activity, the quality of kiwifruit extracts intended for allergy diagnosis can vary in content and amount of IgE reactive molecules. In addition, the quality of allergen extracts for allergy diagnosis depends on the fruit ripening stage and storage conditions. In terms of clinical reactivity, it has become evident that kiwifruit allergy is not a homogeneous disorder. Different patterns of IgE reactivity accompany several clinical subgroups that have been identified in different geographical regions. In the last decade, enormous progress has been made in the isolation and characterization of kiwifruit allergens. This paper presents an overview of the structural features of kiwifruit allergens.
AB  - Od prvog pojavljivanja na tržištu plod kivija je postao izuzetno popularan sastojak humane ishrane usled prijatnog ukusa, niske kalorijske vrednosti i visokog sadržaja vitamina C. Međutim, alergija na kivi je postala učestali uzrok preosetljivosti tipa I u zapadnom društvu. Do sada je otkriveno 11 IgE vezujućih molekula koji čine molekulsku osnovu alergije na kivi. To su proteini i glikoproteini molekulskih masa između 10 i 50 kDa. Glavni alergen kivija je cistein-proteaza označena kao Act d 1, koja sačinjava 50 % rastvornih proteina ploda kivija. Usled razlike u zastupljenosti proteinskih komponenti i biološkoj aktivnosti, kvalitet proteinskih ekstrakata kivija koji se upotrebljavaju u dijagnostifikovanju alergije može varirati u sadržaju i količini IgE reaktivnih molekula. Takođe, kvalitet alergenih ekstrakata zavisi od stepena zrelosti voća prilikom branja, kao i od uslova skladištenja voća nakon branja. Po pitanju kliničke reaktivnosti postalo je očigledno da alergija na plod kivija ne predstavlja homogeni poremećaj. Različiti obrasci IgE reaktivnosti uočeni su kod nekolicine kliničkih podgrupa koje su identifikovane u različitim geografskim regijama. Tokom poslednje decenije načinjen je veliki napredak u izolovanju i karakterizaciji IgE vezujućih proteina kivija. U okviru ovog rada daćemo pregled strukturnih osobina alergenih proteina kivija.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Kiwifruit as a food allergen source
T1  - Plod kivija kao izvor alergena hrane
VL  - 78
IS  - 3
SP  - 333
EP  - 352
DO  - 10.2298/JSC121210011P
ER  - 

@article{
author = "Popović, Milica M. and Grozdanović, Milica and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Since its first appearance on the market, kiwifruit has become very popular in the human diet due to its pleasant taste, low caloric value and high content of vitamin C. However, kiwifruit allergy has become a frequent cause of type I hypersensitivity in the western society. The molecular basis for kiwifruit allergy has been ascribed to up-to-now 11 identified IgE reactive molecules. They are proteins and glycoproteins with a molecular mass between 10 and 50 kDa. The major kiwifruit allergen is a cysteine protease denoted as Act d 1, which represents 50 % of the soluble protein extract. Due to differences in the abundance of the protein components and biological activity, the quality of kiwifruit extracts intended for allergy diagnosis can vary in content and amount of IgE reactive molecules. In addition, the quality of allergen extracts for allergy diagnosis depends on the fruit ripening stage and storage conditions. In terms of clinical reactivity, it has become evident that kiwifruit allergy is not a homogeneous disorder. Different patterns of IgE reactivity accompany several clinical subgroups that have been identified in different geographical regions. In the last decade, enormous progress has been made in the isolation and characterization of kiwifruit allergens. This paper presents an overview of the structural features of kiwifruit allergens., Od prvog pojavljivanja na tržištu plod kivija je postao izuzetno popularan sastojak humane ishrane usled prijatnog ukusa, niske kalorijske vrednosti i visokog sadržaja vitamina C. Međutim, alergija na kivi je postala učestali uzrok preosetljivosti tipa I u zapadnom društvu. Do sada je otkriveno 11 IgE vezujućih molekula koji čine molekulsku osnovu alergije na kivi. To su proteini i glikoproteini molekulskih masa između 10 i 50 kDa. Glavni alergen kivija je cistein-proteaza označena kao Act d 1, koja sačinjava 50 % rastvornih proteina ploda kivija. Usled razlike u zastupljenosti proteinskih komponenti i biološkoj aktivnosti, kvalitet proteinskih ekstrakata kivija koji se upotrebljavaju u dijagnostifikovanju alergije može varirati u sadržaju i količini IgE reaktivnih molekula. Takođe, kvalitet alergenih ekstrakata zavisi od stepena zrelosti voća prilikom branja, kao i od uslova skladištenja voća nakon branja. Po pitanju kliničke reaktivnosti postalo je očigledno da alergija na plod kivija ne predstavlja homogeni poremećaj. Različiti obrasci IgE reaktivnosti uočeni su kod nekolicine kliničkih podgrupa koje su identifikovane u različitim geografskim regijama. Tokom poslednje decenije načinjen je veliki napredak u izolovanju i karakterizaciji IgE vezujućih proteina kivija. U okviru ovog rada daćemo pregled strukturnih osobina alergenih proteina kivija.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Kiwifruit as a food allergen source, Plod kivija kao izvor alergena hrane",
volume = "78",
number = "3",
pages = "333-352",
doi = "10.2298/JSC121210011P"
}

Popović, M. M., Grozdanović, M.,& Gavrović-Jankulović, M.. (2013). Kiwifruit as a food allergen source. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 78(3), 333-352.
https://doi.org/10.2298/JSC121210011P

Popović MM, Grozdanović M, Gavrović-Jankulović M. Kiwifruit as a food allergen source. in Journal of the Serbian Chemical Society. 2013;78(3):333-352.
doi:10.2298/JSC121210011P .

Popović, Milica M., Grozdanović, Milica, Gavrović-Jankulović, Marija, "Kiwifruit as a food allergen source" in Journal of the Serbian Chemical Society, 78, no. 3 (2013):333-352,
https://doi.org/10.2298/JSC121210011P . .

TY  - JOUR
AU  - Čavić, Milena
AU  - Grozdanović, Milica
AU  - Bajić, Aleksandar
AU  - Srdić-Rajić, Tatjana
AU  - Andjus, Pavle R.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1284
AB  - Actinidin belongs to the papain-like family of cysteine proteases and is a major kiwifruit allergen. In this study, the effect of actinidin on cellular morphology and adhesion of T84 intestinal cells was investigated. Both rounding and detachment of T84 cells were observed upon actinidin treatment. The morphological changes and cell desquamation was protease-dependent, as well as time- and concentration-dependent. Changes of intercellular adhesion and adhesion of epithelial cells to collagen upon actinidin treatment could be responsible for the cell rounding and give rise to discontinuous breaches in the epithelial monolayer observed in this study. Actinidin's action on cell morphology, adhesion and monolayer integrity were not due to compromised viability of T84 epithelial cells, as confirmed by MTT assay and flow cytometric analysis of the cell cycle. Damage to the epithelial monolayer of the intestine induced by actinidin should be further evaluated as an important factor in the development of kiwifruit allergy and other intestinal disorders.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells
VL  - 77
SP  - 46
EP  - 52
DO  - 10.1016/j.phytochem.2011.12.014
ER  - 

@article{
author = "Čavić, Milena and Grozdanović, Milica and Bajić, Aleksandar and Srdić-Rajić, Tatjana and Andjus, Pavle R. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Actinidin belongs to the papain-like family of cysteine proteases and is a major kiwifruit allergen. In this study, the effect of actinidin on cellular morphology and adhesion of T84 intestinal cells was investigated. Both rounding and detachment of T84 cells were observed upon actinidin treatment. The morphological changes and cell desquamation was protease-dependent, as well as time- and concentration-dependent. Changes of intercellular adhesion and adhesion of epithelial cells to collagen upon actinidin treatment could be responsible for the cell rounding and give rise to discontinuous breaches in the epithelial monolayer observed in this study. Actinidin's action on cell morphology, adhesion and monolayer integrity were not due to compromised viability of T84 epithelial cells, as confirmed by MTT assay and flow cytometric analysis of the cell cycle. Damage to the epithelial monolayer of the intestine induced by actinidin should be further evaluated as an important factor in the development of kiwifruit allergy and other intestinal disorders.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells",
volume = "77",
pages = "46-52",
doi = "10.1016/j.phytochem.2011.12.014"
}

Čavić, M., Grozdanović, M., Bajić, A., Srdić-Rajić, T., Andjus, P. R.,& Gavrović-Jankulović, M.. (2012). Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells. in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 77, 46-52.
https://doi.org/10.1016/j.phytochem.2011.12.014

Čavić M, Grozdanović M, Bajić A, Srdić-Rajić T, Andjus PR, Gavrović-Jankulović M. Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells. in Phytochemistry. 2012;77:46-52.
doi:10.1016/j.phytochem.2011.12.014 .

Čavić, Milena, Grozdanović, Milica, Bajić, Aleksandar, Srdić-Rajić, Tatjana, Andjus, Pavle R., Gavrović-Jankulović, Marija, "Actinidin, a protease from kiwifruit, induces changes in morphology and adhesion of T84 intestinal epithelial cells" in Phytochemistry, 77 (2012):46-52,
https://doi.org/10.1016/j.phytochem.2011.12.014 . .

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1246
AB  - For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-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 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot 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  - Serbian Chemical Soc, Belgrade
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
VL  - 77
IS  - 1
SP  - 43
EP  - 52
DO  - 10.2298/JSC110309158A
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica M. and Dimitrijevic, Rajna and Burazer, Lidija M. 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 pGEX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 construct were employed for production of the protein induced by 1 mM isopropyl-beta-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 degrees C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of about 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot 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 = "Serbian Chemical Soc, Belgrade",
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",
volume = "77",
number = "1",
pages = "43-52",
doi = "10.2298/JSC110309158A"
}

Abughren, M., Popović, M. M., Dimitrijevic, R., Burazer, L. M., 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
Serbian Chemical Soc, Belgrade., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A

Abughren M, Popović MM, Dimitrijevic R, Burazer LM, 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 M., Dimitrijevic, Rajna, Burazer, Lidija M., 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 M.
AU  - Dimitrijevic, Rajna
AU  - Burazer, Lidija M.
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1259
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)
VL  - 77
IS  - 2
SP  - 257
EP  - 258
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1259
ER  - 

@article{
author = "Abughren, Mohamed and Popović, Milica M. and Dimitrijevic, Rajna and Burazer, Lidija M. and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)",
volume = "77",
number = "2",
pages = "257-258",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1259"
}

Abughren, M., Popović, M. M., Dimitrijevic, R., Burazer, L. M., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(2), 257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259

Abughren M, Popović MM, Dimitrijevic R, Burazer LM, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

Abughren, Mohamed, Popović, Milica M., Dimitrijevic, Rajna, Burazer, Lidija M., Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)" in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
https://hdl.handle.net/21.15107/rcub_cherry_1259 .

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica M.
AU  - Polović, Natalija
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1286
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
VL  - 50
IS  - 3-4
SP  - 1013
EP  - 1018
DO  - 10.1016/j.fct.2011.12.030
ER  - 

@article{
author = "Grozdanović, Milica and Popović, Milica M. and Polović, Natalija and Burazer, Lidija M. 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",
volume = "50",
number = "3-4",
pages = "1013-1018",
doi = "10.1016/j.fct.2011.12.030"
}

Grozdanović, M., Popović, M. M., Polović, N., Burazer, L. M., 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 MM, Polović N, Burazer LM, 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 M., Polović, Natalija, Burazer, Lidija M., 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 . .