TY  - JOUR
AU  - Soković, Marina
AU  - Marin, Petar D.
AU  - Janaćković, Peđa T.
AU  - Vjis, V
AU  - Milosavljevic, S
AU  - Dokovic, D
AU  - Tešević, Vele
AU  - Petrović, S
PY  - 2002
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/490
AB  - Plant material was collected in Bar (Montenegro) in 1997. The essential oils from the leaves of Phlomis fruticosa L. were obtained by hydrodistillation. Forty components were identified by GC/MS analysis. The main components were beta-caryophyllene (12.0%), (E)-methyl isoeugenol (15.3%) and alpha-asarone (10.9%).
PB  - Taylor & Francis Inc, Philadelphia
T2  - Journal of Essential Oil Research
T1  - Composition of the essential oils of Phlomis fruticosa L. (Lamiaceae)
VL  - 14
IS  - 3
SP  - 167
EP  - 168
DO  - 10.1080/10412905.2002.9699812
ER  - 

@article{
author = "Soković, Marina and Marin, Petar D. and Janaćković, Peđa T. and Vjis, V and Milosavljevic, S and Dokovic, D and Tešević, Vele and Petrović, S",
year = "2002",
abstract = "Plant material was collected in Bar (Montenegro) in 1997. The essential oils from the leaves of Phlomis fruticosa L. were obtained by hydrodistillation. Forty components were identified by GC/MS analysis. The main components were beta-caryophyllene (12.0%), (E)-methyl isoeugenol (15.3%) and alpha-asarone (10.9%).",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Journal of Essential Oil Research",
title = "Composition of the essential oils of Phlomis fruticosa L. (Lamiaceae)",
volume = "14",
number = "3",
pages = "167-168",
doi = "10.1080/10412905.2002.9699812"
}

Soković, M., Marin, P. D., Janaćković, P. T., Vjis, V., Milosavljevic, S., Dokovic, D., Tešević, V.,& Petrović, S.. (2002). Composition of the essential oils of Phlomis fruticosa L. (Lamiaceae). in Journal of Essential Oil Research
Taylor & Francis Inc, Philadelphia., 14(3), 167-168.
https://doi.org/10.1080/10412905.2002.9699812

Soković M, Marin PD, Janaćković PT, Vjis V, Milosavljevic S, Dokovic D, Tešević V, Petrović S. Composition of the essential oils of Phlomis fruticosa L. (Lamiaceae). in Journal of Essential Oil Research. 2002;14(3):167-168.
doi:10.1080/10412905.2002.9699812 .

Soković, Marina, Marin, Petar D., Janaćković, Peđa T., Vjis, V, Milosavljevic, S, Dokovic, D, Tešević, Vele, Petrović, S, "Composition of the essential oils of Phlomis fruticosa L. (Lamiaceae)" in Journal of Essential Oil Research, 14, no. 3 (2002):167-168,
https://doi.org/10.1080/10412905.2002.9699812 . .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Bukilica, M
AU  - Fahlbusch, B
AU  - Petrović, S
AU  - Jankov, Ratko M.
PY  - 2000
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/447
AB  - More than 75% of grass pollen-allergic patients produce specific IgE antibodies against group-4 allergens. Purification and characterization of different grass group-4 allergens should help to further understand their allergenicity. In this study, an attempt was made to isolate and characterize Fes p 4 allergen by several biochemical and immunochemical methods. Fes p 4 was purified by a combination of chromatographic techniques (gel permeation and ion exchange chromatography). Isolated protein revealed four main spots at a molecular weight of 60 kDa and a pi ranging from 8.7 to 9.1. Eight sera were selected from patients with positive result of skin prick test to the mixture of grass pollen extracts. ELISA inhibition technique was used to study Fes p 4-specific IgE in the patients' sera. ELISA to Festuca pratensis was inhibited up to 80% by F. pratensis pollen extract and up to 48% by Fes p 4. 2D-PAGE-immunoblot was used to identify allergenic and antigenic components of Fes p 4 with patients' IgE and monoclonal antibodies (MABs). Three components of purified protein expressed IgE binding ability. Two MABs which recognized unrelated regions on Phl p 4 bound three components of Fes p 4. The role of the carbohydrate moiety in allergenicity was examined with individual patient sera by using periodate-treated Fes p 4. Six out of eight patients reduced IgE binding to periodate-treated allergen. Isolated Fes p 4 glycoprotein consisted of four components, three of which were allergenic, and share common epitopes specific for grass group-4 homologs. The results of periodate oxidation of Fes p 4 suggest that the carbohydrate moiety is involved in IgE binding.
PB  - Prous Science, Sa, Barcelona
T2  - Journal of Investigational Allergology and Clinical Immunology
T1  - Isolation and partial characterization of Fes p 4 allergen
VL  - 10
IS  - 6
SP  - 361
EP  - 367
UR  - https://hdl.handle.net/21.15107/rcub_cherry_447
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Bukilica, M and Fahlbusch, B and Petrović, S and Jankov, Ratko M.",
year = "2000",
abstract = "More than 75% of grass pollen-allergic patients produce specific IgE antibodies against group-4 allergens. Purification and characterization of different grass group-4 allergens should help to further understand their allergenicity. In this study, an attempt was made to isolate and characterize Fes p 4 allergen by several biochemical and immunochemical methods. Fes p 4 was purified by a combination of chromatographic techniques (gel permeation and ion exchange chromatography). Isolated protein revealed four main spots at a molecular weight of 60 kDa and a pi ranging from 8.7 to 9.1. Eight sera were selected from patients with positive result of skin prick test to the mixture of grass pollen extracts. ELISA inhibition technique was used to study Fes p 4-specific IgE in the patients' sera. ELISA to Festuca pratensis was inhibited up to 80% by F. pratensis pollen extract and up to 48% by Fes p 4. 2D-PAGE-immunoblot was used to identify allergenic and antigenic components of Fes p 4 with patients' IgE and monoclonal antibodies (MABs). Three components of purified protein expressed IgE binding ability. Two MABs which recognized unrelated regions on Phl p 4 bound three components of Fes p 4. The role of the carbohydrate moiety in allergenicity was examined with individual patient sera by using periodate-treated Fes p 4. Six out of eight patients reduced IgE binding to periodate-treated allergen. Isolated Fes p 4 glycoprotein consisted of four components, three of which were allergenic, and share common epitopes specific for grass group-4 homologs. The results of periodate oxidation of Fes p 4 suggest that the carbohydrate moiety is involved in IgE binding.",
publisher = "Prous Science, Sa, Barcelona",
journal = "Journal of Investigational Allergology and Clinical Immunology",
title = "Isolation and partial characterization of Fes p 4 allergen",
volume = "10",
number = "6",
pages = "361-367",
url = "https://hdl.handle.net/21.15107/rcub_cherry_447"
}

Gavrović-Jankulović, M., Ćirković-Veličković, T., Bukilica, M., Fahlbusch, B., Petrović, S.,& Jankov, R. M.. (2000). Isolation and partial characterization of Fes p 4 allergen. in Journal of Investigational Allergology and Clinical Immunology
Prous Science, Sa, Barcelona., 10(6), 361-367.
https://hdl.handle.net/21.15107/rcub_cherry_447

Gavrović-Jankulović M, Ćirković-Veličković T, Bukilica M, Fahlbusch B, Petrović S, Jankov RM. Isolation and partial characterization of Fes p 4 allergen. in Journal of Investigational Allergology and Clinical Immunology. 2000;10(6):361-367.
https://hdl.handle.net/21.15107/rcub_cherry_447 .

Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Bukilica, M, Fahlbusch, B, Petrović, S, Jankov, Ratko M., "Isolation and partial characterization of Fes p 4 allergen" in Journal of Investigational Allergology and Clinical Immunology, 10, no. 6 (2000):361-367,
https://hdl.handle.net/21.15107/rcub_cherry_447 .

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Bukilica, MN
AU  - Gavrović-Jankulović, Marija
AU  - Vujčić, Zoran
AU  - Petrović, S
AU  - Jankov, Ratko M.
PY  - 1999
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/411
AB  - Background: Orchard grass (Dactylis glomerata) pollen proteins were chemically modified by means of acid anhydrides (maleic and succinic anhydride) to obtain low-molecular-weight allergoids. Chemical modification in both cases led to the replacement of one positive charge (epsilon amino group of Lys) by one negative charge, yielding proteins with changed physicochemical properties in comparison to the native orchard grass-pollen proteins. Methods: Physicochemical characterization of derivatives was done by gel chromatography, SDS-PAGE, and isoelectric focusing. To examine the IgE-binding properties of these derivatives, we carried out immunoblotting. To examine the ability of derivatives to induce IgG production, we immunized rabbits. Skin prick testing with the allergoids was performed on 15 individuals allergic to orchard grass pollens and on two healthy subjects. Results: II was shown that the modified proteins retain their original molecular weights, but change pi to more acidic values. In the case of allergoids, a strong reduction in IgE binding was found. Immunization of rabbits with allergoids showed that the derivatives retain the ability to induce IgG production, and that the antisera obtained in such a way react to native (unmodified) extract. The ability of derivatives to induce allergic reaction was significantly reduced. The patients (86.6%) included in our study exhibited less than 50% of native extract response. Among them, 53.3% had no response to one or both allergoids. Conclusions: These modification procedures yield allergoids with a reduced allergenic activity and preserved immunogenic potential suitable for use in immunotherapy.
PB  - Munksgaard Int Publ Ltd, Copenhagen
T2  - Allergy
T1  - Physicochemical and immunologic characterization of low molecular-weight allergoids of Dactylis glomerata pollen proteins
VL  - 54
IS  - 2
SP  - 128
EP  - 134
DO  - 10.1034/j.1398-9995.1999.00778.x
ER  - 

@article{
author = "Ćirković-Veličković, Tanja and Bukilica, MN and Gavrović-Jankulović, Marija and Vujčić, Zoran and Petrović, S and Jankov, Ratko M.",
year = "1999",
abstract = "Background: Orchard grass (Dactylis glomerata) pollen proteins were chemically modified by means of acid anhydrides (maleic and succinic anhydride) to obtain low-molecular-weight allergoids. Chemical modification in both cases led to the replacement of one positive charge (epsilon amino group of Lys) by one negative charge, yielding proteins with changed physicochemical properties in comparison to the native orchard grass-pollen proteins. Methods: Physicochemical characterization of derivatives was done by gel chromatography, SDS-PAGE, and isoelectric focusing. To examine the IgE-binding properties of these derivatives, we carried out immunoblotting. To examine the ability of derivatives to induce IgG production, we immunized rabbits. Skin prick testing with the allergoids was performed on 15 individuals allergic to orchard grass pollens and on two healthy subjects. Results: II was shown that the modified proteins retain their original molecular weights, but change pi to more acidic values. In the case of allergoids, a strong reduction in IgE binding was found. Immunization of rabbits with allergoids showed that the derivatives retain the ability to induce IgG production, and that the antisera obtained in such a way react to native (unmodified) extract. The ability of derivatives to induce allergic reaction was significantly reduced. The patients (86.6%) included in our study exhibited less than 50% of native extract response. Among them, 53.3% had no response to one or both allergoids. Conclusions: These modification procedures yield allergoids with a reduced allergenic activity and preserved immunogenic potential suitable for use in immunotherapy.",
publisher = "Munksgaard Int Publ Ltd, Copenhagen",
journal = "Allergy",
title = "Physicochemical and immunologic characterization of low molecular-weight allergoids of Dactylis glomerata pollen proteins",
volume = "54",
number = "2",
pages = "128-134",
doi = "10.1034/j.1398-9995.1999.00778.x"
}

Ćirković-Veličković, T., Bukilica, M., Gavrović-Jankulović, M., Vujčić, Z., Petrović, S.,& Jankov, R. M.. (1999). Physicochemical and immunologic characterization of low molecular-weight allergoids of Dactylis glomerata pollen proteins. in Allergy
Munksgaard Int Publ Ltd, Copenhagen., 54(2), 128-134.
https://doi.org/10.1034/j.1398-9995.1999.00778.x

Ćirković-Veličković T, Bukilica M, Gavrović-Jankulović M, Vujčić Z, Petrović S, Jankov RM. Physicochemical and immunologic characterization of low molecular-weight allergoids of Dactylis glomerata pollen proteins. in Allergy. 1999;54(2):128-134.
doi:10.1034/j.1398-9995.1999.00778.x .

Ćirković-Veličković, Tanja, Bukilica, MN, Gavrović-Jankulović, Marija, Vujčić, Zoran, Petrović, S, Jankov, Ratko M., "Physicochemical and immunologic characterization of low molecular-weight allergoids of Dactylis glomerata pollen proteins" in Allergy, 54, no. 2 (1999):128-134,
https://doi.org/10.1034/j.1398-9995.1999.00778.x . .

TY  - CONF
AU  - Vujčić, Zoran
AU  - Vidojevic, S.
AU  - Petrović, S.
AU  - Jankov, Ratko M.
PY  - 1990
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/18
C3  - Periodicum Biologorum
T1  - Separation and characterisation of Populus canadensis pollen antigens
VL  - 92
IS  - 1
SP  - 58
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_18
ER  - 

@conference{
author = "Vujčić, Zoran and Vidojevic, S. and Petrović, S. and Jankov, Ratko M.",
year = "1990",
journal = "Periodicum Biologorum",
title = "Separation and characterisation of Populus canadensis pollen antigens",
volume = "92",
number = "1",
pages = "58-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_18"
}

Vujčić, Z., Vidojevic, S., Petrović, S.,& Jankov, R. M.. (1990). Separation and characterisation of Populus canadensis pollen antigens. in Periodicum Biologorum, 92(1), 58-59.
https://hdl.handle.net/21.15107/rcub_cherry_18

Vujčić Z, Vidojevic S, Petrović S, Jankov RM. Separation and characterisation of Populus canadensis pollen antigens. in Periodicum Biologorum. 1990;92(1):58-59.
https://hdl.handle.net/21.15107/rcub_cherry_18 .

Vujčić, Zoran, Vidojevic, S., Petrović, S., Jankov, Ratko M., "Separation and characterisation of Populus canadensis pollen antigens" in Periodicum Biologorum, 92, no. 1 (1990):58-59,
https://hdl.handle.net/21.15107/rcub_cherry_18 .