TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan M.
AU  - Živković, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2236
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan M. and Živković, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}

Mrkić, I., Minić, R., Popović, D. M., Živković, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Pergamon-Elsevier Science Ltd, Oxford., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036

Mrkić I, Minić R, Popović DM, Živković I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .

Mrkić, Ivan, Minić, Rajna, Popović, Dragan M., Živković, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan M.
AU  - Živković, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2887
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Elsevier
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
VL  - 213
SP  - 158
EP  - 165
DO  - 10.1016/j.lfs.2018.10.036
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan M. and Živković, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Elsevier",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
volume = "213",
pages = "158-165",
doi = "10.1016/j.lfs.2018.10.036"
}

Mrkić, I., Minić, R., Popović, D. M., Živković, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Elsevier., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036

Mrkić I, Minić R, Popović DM, Živković I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .

Mrkić, Ivan, Minić, Rajna, Popović, Dragan M., Živković, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Bulat, Tanja
AU  - Aradska, Jana
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2472
AB  - BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera
VL  - 92
IS  - 6
SP  - 1328
EP  - 1335
DO  - 10.1002/jctb.5127
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Bulat, Tanja and Aradska, Jana and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera",
volume = "92",
number = "6",
pages = "1328-1335",
doi = "10.1002/jctb.5127"
}

Mrkić, I., Minić, R., Bulat, T., Aradska, J., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology
Wiley, Hoboken., 92(6), 1328-1335.
https://doi.org/10.1002/jctb.5127

Mrkić I, Minić R, Bulat T, Aradska J, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology. 2017;92(6):1328-1335.
doi:10.1002/jctb.5127 .

Mrkić, Ivan, Minić, Rajna, Bulat, Tanja, Aradska, Jana, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera" in Journal of Chemical Technology and Biotechnology, 92, no. 6 (2017):1328-1335,
https://doi.org/10.1002/jctb.5127 . .

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  - Mrkić, Ivan
AU  - Abughren, Mohamed
AU  - Nikolić, Jasna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1774
AB  - Allergy to banana fruit appears to have become an important cause of fruit allergy in Europe. Among five allergens that have been found, beta-1,3-glucanase denoted as Mus a 5 was identified as a candidate allergen for the component-resolved allergy diagnosis of banana allergy. Because of the variations in protein levels in banana fruit, in this study Mus a 5 was produced as a fusion protein with glutathione-S-transferase in Escherichia coli. The recombinant Mus a 5 was purified under native conditions by a combination of affinity, ion-exchange, and reversed phase chromatography. N-terminal sequence was confirmed by Edman degradation and 55 % of the primary structure was identified by mass fingerprint, while the secondary structure was assessed by circular dichroism spectroscopy. IgG reactivity of recombinant protein was shown in 2-D immunoblot with anti-Mus a 5 antibodies, while IgG and IgE binding to natural Mus a 5 was inhibited with the recombinant Mus a 5 in immunoblot inhibition test. IgE reactivity of recombinant Mus a 5 was shown in ELISA within a group of ten persons sensitized to banana fruit. Recombinant Mus a 5 is a novel reagent suitable for the component-resolved allergy diagnosis of banana allergy.
PB  - Humana Press Inc, Totowa
T2  - Molecular Biotechnology
T1  - Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit
VL  - 56
IS  - 6
SP  - 498
EP  - 506
DO  - 10.1007/s12033-013-9719-8
ER  - 

@article{
author = "Mrkić, Ivan and Abughren, Mohamed and Nikolić, Jasna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "Allergy to banana fruit appears to have become an important cause of fruit allergy in Europe. Among five allergens that have been found, beta-1,3-glucanase denoted as Mus a 5 was identified as a candidate allergen for the component-resolved allergy diagnosis of banana allergy. Because of the variations in protein levels in banana fruit, in this study Mus a 5 was produced as a fusion protein with glutathione-S-transferase in Escherichia coli. The recombinant Mus a 5 was purified under native conditions by a combination of affinity, ion-exchange, and reversed phase chromatography. N-terminal sequence was confirmed by Edman degradation and 55 % of the primary structure was identified by mass fingerprint, while the secondary structure was assessed by circular dichroism spectroscopy. IgG reactivity of recombinant protein was shown in 2-D immunoblot with anti-Mus a 5 antibodies, while IgG and IgE binding to natural Mus a 5 was inhibited with the recombinant Mus a 5 in immunoblot inhibition test. IgE reactivity of recombinant Mus a 5 was shown in ELISA within a group of ten persons sensitized to banana fruit. Recombinant Mus a 5 is a novel reagent suitable for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Humana Press Inc, Totowa",
journal = "Molecular Biotechnology",
title = "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit",
volume = "56",
number = "6",
pages = "498-506",
doi = "10.1007/s12033-013-9719-8"
}

Mrkić, I., Abughren, M., Nikolić, J., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2014). Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology
Humana Press Inc, Totowa., 56(6), 498-506.
https://doi.org/10.1007/s12033-013-9719-8

Mrkić I, Abughren M, Nikolić J, Anđelković U, Vassilopoulou E, Sinaniotis A, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit. in Molecular Biotechnology. 2014;56(6):498-506.
doi:10.1007/s12033-013-9719-8 .

Mrkić, Ivan, Abughren, Mohamed, Nikolić, Jasna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular Characterization of Recombinant Mus a 5 Allergen from Banana Fruit" in Molecular Biotechnology, 56, no. 6 (2014):498-506,
https://doi.org/10.1007/s12033-013-9719-8 . .

TY  - JOUR
AU  - Vujisić, Ljubodrag V.
AU  - Vučković, Ivan M.
AU  - Makarov, Slobodan E.
AU  - Ilić, Bojan S.
AU  - Antić, Dragan Ž.
AU  - Jadranin, Milka
AU  - Todorović, Nina
AU  - Mrkić, Ivan
AU  - Vajs, Vlatka
AU  - Lučić, Luka
AU  - Ćurčić, Božidar P. M.
AU  - Mitić, Bojan M.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1394
AB  - The geophilomorph centipede, Himantarium gabrielis, when disturbed, discharges a viscous and proteinaceous secretion from the sternal glands. This exudate was found by gas chromatography-mass spectrometry, liquid chromatography-high resolution mass spectrometry, liquid chromatography-mass spectrometry-mass spectrometry and NMR analyses to be composed of hydrogen cyanide, benzaldehyde, benzoyl nitrile, benzyl nitrile, mandelonitrile, mandelonitrile benzoate, 3,7,6O-trimethylguanine (himantarine), farnesyl 2,3-dihydrofarnesoate and farnesyl farnesoate. This is the first report on the presence of benzyl nitrile and mandelonitrile benzoate in secreted substances from centipedes. Farnesyl 2,3-dihydrofarnesoate is a new compound, while himantarine and farnesyl farnesoate were not known as natural products. A post-secretion release of hydrogen cyanide by reaction of mandelonitrile and benzoyl nitrile was observed by NMR, and hydrogen cyanide signals were completely assigned. In addition, a protein component of the secretion was analysed by electrophoresis which revealed the presence of a major 55 kDa protein. Analyses of the defensive exudates of other geophilomorph families should produce further chemical surprises.
PB  - Springer, New York
T2  - Naturwissenschaften
T1  - Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)
VL  - 100
IS  - 9
SP  - 861
EP  - 870
DO  - 10.1007/s00114-013-1086-6
ER  - 

@article{
author = "Vujisić, Ljubodrag V. and Vučković, Ivan M. and Makarov, Slobodan E. and Ilić, Bojan S. and Antić, Dragan Ž. and Jadranin, Milka and Todorović, Nina and Mrkić, Ivan and Vajs, Vlatka and Lučić, Luka and Ćurčić, Božidar P. M. and Mitić, Bojan M.",
year = "2013",
abstract = "The geophilomorph centipede, Himantarium gabrielis, when disturbed, discharges a viscous and proteinaceous secretion from the sternal glands. This exudate was found by gas chromatography-mass spectrometry, liquid chromatography-high resolution mass spectrometry, liquid chromatography-mass spectrometry-mass spectrometry and NMR analyses to be composed of hydrogen cyanide, benzaldehyde, benzoyl nitrile, benzyl nitrile, mandelonitrile, mandelonitrile benzoate, 3,7,6O-trimethylguanine (himantarine), farnesyl 2,3-dihydrofarnesoate and farnesyl farnesoate. This is the first report on the presence of benzyl nitrile and mandelonitrile benzoate in secreted substances from centipedes. Farnesyl 2,3-dihydrofarnesoate is a new compound, while himantarine and farnesyl farnesoate were not known as natural products. A post-secretion release of hydrogen cyanide by reaction of mandelonitrile and benzoyl nitrile was observed by NMR, and hydrogen cyanide signals were completely assigned. In addition, a protein component of the secretion was analysed by electrophoresis which revealed the presence of a major 55 kDa protein. Analyses of the defensive exudates of other geophilomorph families should produce further chemical surprises.",
publisher = "Springer, New York",
journal = "Naturwissenschaften",
title = "Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)",
volume = "100",
number = "9",
pages = "861-870",
doi = "10.1007/s00114-013-1086-6"
}

Vujisić, L. V., Vučković, I. M., Makarov, S. E., Ilić, B. S., Antić, D. Ž., Jadranin, M., Todorović, N., Mrkić, I., Vajs, V., Lučić, L., Ćurčić, B. P. M.,& Mitić, B. M.. (2013). Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae). in Naturwissenschaften
Springer, New York., 100(9), 861-870.
https://doi.org/10.1007/s00114-013-1086-6

Vujisić LV, Vučković IM, Makarov SE, Ilić BS, Antić DŽ, Jadranin M, Todorović N, Mrkić I, Vajs V, Lučić L, Ćurčić BPM, Mitić BM. Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae). in Naturwissenschaften. 2013;100(9):861-870.
doi:10.1007/s00114-013-1086-6 .

Vujisić, Ljubodrag V., Vučković, Ivan M., Makarov, Slobodan E., Ilić, Bojan S., Antić, Dragan Ž., Jadranin, Milka, Todorović, Nina, Mrkić, Ivan, Vajs, Vlatka, Lučić, Luka, Ćurčić, Božidar P. M., Mitić, Bojan M., "Chemistry of the sternal gland secretion of the Mediterranean centipede Himantarium gabrielis (Linnaeus, 1767) (Chilopoda: Geophilomorpha: Himantariidae)" in Naturwissenschaften, 100, no. 9 (2013):861-870,
https://doi.org/10.1007/s00114-013-1086-6 . .

TY  - JOUR
AU  - Macinkovic, Igor S.
AU  - Abughren, Mohamed
AU  - Mrkić, Ivan
AU  - Grozdanović, Milica M.
AU  - Prodanović, Radivoje
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1449
AB  - High levels of recombinant protein expression can lead to the formation of insoluble inclusion bodies. These complex aggregates are commonly solubilized in strong denaturants, such as 6-8 M urea, although, if possible, solubilization under milder conditions could facilitate subsequent refolding and purification of bioactive proteins. Commercially available GST-tag assays are designed for quantitative measurement of GST activity under native conditions. GST fusion proteins accumulated in inclusion bodies are considered to be undetectable by such assays. In this work, solubilization of recombinantly produced proteins was performed in 4 M urea. The activity of rGST was assayed in 2 M urea and it was shown that rGST preserves 85% of its activity under such denaturing conditions. A colorimetric GST activity assay with 1-chloro-2, 4-dinitrobenzene (CDNB) was examined for use in rapid detection of expression targeted to inclusion bodies and for the identification of inclusion body proteins which can be solubilized in low concentrations of chaotropic agents. Applicability of the assay was evaluated by tracking protein expression of two GST-fused allergens of biopharmaceutical value in E. coli, GST-Der p 2 and GST-Mus a 5, both targeted to inclusion bodies.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Biotechnology
T1  - Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies
VL  - 168
IS  - 4
SP  - 506
EP  - 510
DO  - 10.1016/j.jbiotec.2013.09.019
ER  - 

@article{
author = "Macinkovic, Igor S. and Abughren, Mohamed and Mrkić, Ivan and Grozdanović, Milica M. and Prodanović, Radivoje and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "High levels of recombinant protein expression can lead to the formation of insoluble inclusion bodies. These complex aggregates are commonly solubilized in strong denaturants, such as 6-8 M urea, although, if possible, solubilization under milder conditions could facilitate subsequent refolding and purification of bioactive proteins. Commercially available GST-tag assays are designed for quantitative measurement of GST activity under native conditions. GST fusion proteins accumulated in inclusion bodies are considered to be undetectable by such assays. In this work, solubilization of recombinantly produced proteins was performed in 4 M urea. The activity of rGST was assayed in 2 M urea and it was shown that rGST preserves 85% of its activity under such denaturing conditions. A colorimetric GST activity assay with 1-chloro-2, 4-dinitrobenzene (CDNB) was examined for use in rapid detection of expression targeted to inclusion bodies and for the identification of inclusion body proteins which can be solubilized in low concentrations of chaotropic agents. Applicability of the assay was evaluated by tracking protein expression of two GST-fused allergens of biopharmaceutical value in E. coli, GST-Der p 2 and GST-Mus a 5, both targeted to inclusion bodies.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies",
volume = "168",
number = "4",
pages = "506-510",
doi = "10.1016/j.jbiotec.2013.09.019"
}

Macinkovic, I. S., Abughren, M., Mrkić, I., Grozdanović, M. M., Prodanović, R.,& Gavrović-Jankulović, M.. (2013). Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam., 168(4), 506-510.
https://doi.org/10.1016/j.jbiotec.2013.09.019

Macinkovic IS, Abughren M, Mrkić I, Grozdanović MM, Prodanović R, Gavrović-Jankulović M. Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies. in Journal of Biotechnology. 2013;168(4):506-510.
doi:10.1016/j.jbiotec.2013.09.019 .

Macinkovic, Igor S., Abughren, Mohamed, Mrkić, Ivan, Grozdanović, Milica M., Prodanović, Radivoje, Gavrović-Jankulović, Marija, "Employment of colorimetric enzyme assay for monitoring expression and solubility of GST fusion proteins targeted to inclusion bodies" in Journal of Biotechnology, 168, no. 4 (2013):506-510,
https://doi.org/10.1016/j.jbiotec.2013.09.019 . .

TY  - JOUR
AU  - Jovanović, Rada
AU  - Mrkić, Ivan
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/170
AB  - Xanthophylls are isoprenoid oxygen compounds with long polyene chain containing up to 13 conjugated double bonds. At both ends of a xanthophyll molecule is a ring. Xanthophylls are natural pigments produced in plants, whose role is to protect the photosynthetic apparatus, and which represent the color of the fruits. Also, xanthophylls are provitamins A. In following text are explained the structure and biosynthesis of xanthophylls, their role in plant and animal kingdom with focus on their antioxidant and fotoprotective effect.
AB  - Ksantofili su izoprenoidi sa dugačkim polienskim lancem koji sadrži do 13 konjugovanih dvostrukih veza i funkcionalnu grupu sa kiseonikom. Na oba kraja molekula ksantofila nalazi se prsten. Ksantofili su prirodni pigmenti koji se sintetišu u biljkama, daju boju plodovima i imaju ulogu i zaštiti fotosintetičkog aparata. U daljem tekstu objašnjena je biosinteza i struktura ksantofila, kao i njihova uloga u biljnom i životinjskom svetu sa akcentom na njihovo antioksidativno i fotoprotektivno dejstvo.
T2  - Hemijski pregled
T1  - Structures and roles
T1  - Ksantofili - srukture i uloge
VL  - 54
IS  - 3
SP  - 74
EP  - 77
UR  - https://hdl.handle.net/21.15107/rcub_cherry_170
ER  - 

@article{
author = "Jovanović, Rada and Mrkić, Ivan",
year = "2013",
abstract = "Xanthophylls are isoprenoid oxygen compounds with long polyene chain containing up to 13 conjugated double bonds. At both ends of a xanthophyll molecule is a ring. Xanthophylls are natural pigments produced in plants, whose role is to protect the photosynthetic apparatus, and which represent the color of the fruits. Also, xanthophylls are provitamins A. In following text are explained the structure and biosynthesis of xanthophylls, their role in plant and animal kingdom with focus on their antioxidant and fotoprotective effect., Ksantofili su izoprenoidi sa dugačkim polienskim lancem koji sadrži do 13 konjugovanih dvostrukih veza i funkcionalnu grupu sa kiseonikom. Na oba kraja molekula ksantofila nalazi se prsten. Ksantofili su prirodni pigmenti koji se sintetišu u biljkama, daju boju plodovima i imaju ulogu i zaštiti fotosintetičkog aparata. U daljem tekstu objašnjena je biosinteza i struktura ksantofila, kao i njihova uloga u biljnom i životinjskom svetu sa akcentom na njihovo antioksidativno i fotoprotektivno dejstvo.",
journal = "Hemijski pregled",
title = "Structures and roles, Ksantofili - srukture i uloge",
volume = "54",
number = "3",
pages = "74-77",
url = "https://hdl.handle.net/21.15107/rcub_cherry_170"
}

Jovanović, R.,& Mrkić, I.. (2013). Structures and roles. in Hemijski pregled, 54(3), 74-77.
https://hdl.handle.net/21.15107/rcub_cherry_170

Jovanović R, Mrkić I. Structures and roles. in Hemijski pregled. 2013;54(3):74-77.
https://hdl.handle.net/21.15107/rcub_cherry_170 .

Jovanović, Rada, Mrkić, Ivan, "Structures and roles" in Hemijski pregled, 54, no. 3 (2013):74-77,
https://hdl.handle.net/21.15107/rcub_cherry_170 .