TY  - JOUR
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Petrušić, Vladimir
AU  - Kosec, Duško
AU  - Dimitrijević, Rajna
AU  - Jankov, Ratko
AU  - Dimitrijević, Ljiljana
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/300
AB  - Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved
PB  - Elsevier, Amsterdam
T2  - International Immunopharmacology
T1  - In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma
EP  - 129
IS  - 1
SP  - 120
VL  - 10
DO  - 10.1016/j.intimp.2009.10.007
ER  - 

@article{
author = "Stojanović, Marijana and Živković, Irena and Petrušić, Vladimir and Kosec, Duško and Dimitrijević, Rajna and Jankov, Ratko and Dimitrijević, Ljiljana and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Lectins are widely used in many types of assay but some lectins such as banana lectin (BanLec) are recognised as potent immunostimulators Although BanLec's structure and binding characteristics are now familiar, its immunostimulatory potential has not yet been fully explored The synthesis by recombinant technology of a BanLec isoform (rBanLec) whose binding properties are similar to its natural counterpart has made it possible to overcome the twin problems of natural BanLec's microheterogeneity and low availability This study's aim is to explore the immunostimulatory potential of rBanLec in the murine model Analyses of the responses of Balb/c- and C57 BL/6-originated splenocytes to in vitro rBanLec stimulation were performed to examine the dependency of rBanLec's immunostimulatory potential upon the splenocytes' genetic background It is shown that the responses of Balb/c- and C57 BL/6-originated splenocytes to rBanLec stimulation differ both qualitatively and in intensity. The hallmarks of the induced responses are T lymphocyte proliferation and intensive interferon-gamma secretion Both phenomena are more marked in Balb/c-originated cultures; Balb/c-originated lymphocytes produce interleukin (IL)-4 and IL-10 following rBanLec stimulation Out results demonstrate that any responses to rBanLec stimulation are highly dependent upon genetic background. they suggest that genetic background must be an important consideration in any further investigations using animal models or when exploring rBanLec's potential human applications (C) 2009 Elsevier B V. All rights reserved",
publisher = "Elsevier, Amsterdam",
journal = "International Immunopharmacology",
title = "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma",
pages = "129-120",
number = "1",
volume = "10",
doi = "10.1016/j.intimp.2009.10.007"
}

Stojanović, M., Živković, I., Petrušić, V., Kosec, D., Dimitrijević, R., Jankov, R., Dimitrijević, L.,& Gavrović-Jankulović, M.. (2010). In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology
Elsevier, Amsterdam., 10(1), 120-129.
https://doi.org/10.1016/j.intimp.2009.10.007

Stojanović M, Živković I, Petrušić V, Kosec D, Dimitrijević R, Jankov R, Dimitrijević L, Gavrović-Jankulović M. In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma. in International Immunopharmacology. 2010;10(1):120-129.
doi:10.1016/j.intimp.2009.10.007 .

Stojanović, Marijana, Živković, Irena, Petrušić, Vladimir, Kosec, Duško, Dimitrijević, Rajna, Jankov, Ratko, Dimitrijević, Ljiljana, Gavrović-Jankulović, Marija, "In vitro stimulation of Balb/c and C57 BL/6 splenocytes by a recombinantly produced banana lectin isoform results in both a proliferation of T cells and an increased secretion of interferon-gamma" in International Immunopharmacology, 10, no. 1 (2010):120-129,
https://doi.org/10.1016/j.intimp.2009.10.007 . .

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  - Dimitrijević, Rajna
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Dimitrijević, Ljiljana
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/275
AB  - Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
EP  - 2115
IS  - 6
SP  - 2108
VL  - 107
DO  - 10.1111/j.1365-2672.2009.04539.x
ER  - 

@article{
author = "Dimitrijević, Rajna and Stojanović, Marijana and Živković, Irena and Petersen, Arnd and Jankov, Ratko and Dimitrijević, Ljiljana and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
pages = "2115-2108",
number = "6",
volume = "107",
doi = "10.1111/j.1365-2672.2009.04539.x"
}

Dimitrijević, R., Stojanović, M., Živković, I., Petersen, A., Jankov, R., Dimitrijević, L.,& Gavrović-Jankulović, M.. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology
Wiley, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x

Dimitrijević R, Stojanović M, Živković I, Petersen A, Jankov R, Dimitrijević L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology. 2009;107(6):2108-2115.
doi:10.1111/j.1365-2672.2009.04539.x .

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

TY  - 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  - JOUR
AU  - Milovanović, Katarina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/285
AB  - House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment.
AB  - Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus
T1  - Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja
EP  - 522
IS  - 5
SP  - 513
VL  - 74
DO  - 10.2298/JSC0905513M
ER  - 

@article{
author = "Milovanović, Katarina and Burazer, Lidija and Vučković, Olga and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment., Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus, Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja",
pages = "522-513",
number = "5",
volume = "74",
doi = "10.2298/JSC0905513M"
}

Milovanović, K., Burazer, L., Vučković, O., Atanasković-Marković, M., Ćirković-Veličković, T., Jankov, R.,& Gavrović-Jankulović, M.. (2009). Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 74(5), 513-522.
https://doi.org/10.2298/JSC0905513M

Milovanović K, Burazer L, Vučković O, Atanasković-Marković M, Ćirković-Veličković T, Jankov R, Gavrović-Jankulović M. Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society. 2009;74(5):513-522.
doi:10.2298/JSC0905513M .

Milovanović, Katarina, Burazer, Lidija, Vučković, Olga, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, Jankov, Ratko, Gavrović-Jankulović, Marija, "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus" in Journal of the Serbian Chemical Society, 74, no. 5 (2009):513-522,
https://doi.org/10.2298/JSC0905513M . .

TY  - JOUR
AU  - Perović, I.
AU  - Milovanović, Mina
AU  - Stanić, Dragana
AU  - Burazer, Lidija
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelink, G.
AU  - van Hage, Marianne
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/270
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
EP  - 446
IS  - 3
SP  - 435
VL  - 39
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perović, I. and Milovanović, Mina and Stanić, Dragana and Burazer, Lidija and Petrović, D. and Milčić-Matić, Natalija and Gafvelink, G. and van Hage, Marianne and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
pages = "446-435",
number = "3",
volume = "39",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perović, I., Milovanović, M., Stanić, D., Burazer, L., Petrović, D., Milčić-Matić, N., Gafvelink, G., van Hage, M., Jankov, R.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley, Hoboken., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perović I, Milovanović M, Stanić D, Burazer L, Petrović D, Milčić-Matić N, Gafvelink G, van Hage M, Jankov R, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perović, I., Milovanović, Mina, Stanić, Dragana, Burazer, Lidija, Petrović, D., Milčić-Matić, Natalija, Gafvelink, G., van Hage, Marianne, Jankov, Ratko, Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/286
AB  - Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v 1 that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified amino groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids.
AB  - Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation
T1  - Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem
EP  - 366
IS  - 4
SP  - 359
VL  - 74
DO  - 10.2298/JSC0904359S
ER  - 

@article{
author = "Stanić, Dragana and Burazer, Lidija and Gavrović-Jankulović, Marija and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Art v 1 is the major allergen of mugwort (Artemisia vulgaris) pollen, a significant cause of hay fever all over Europe. Specific immunotherapy is the only treatment modality for allergic disease. Application of modified allergens makes the treatment safer and more efficient. In this work, two out of three (citraconic anhydride, cis-aconitic anhydride, 2,3-dimethylmaleic anhydride) tested anhydrides were proven to be suitable for chemical modifications of allergens. Art v 1 was modified by cis-aconitylation and citraconylation in order to obtain derivatives of Art v 1 that may be suitable for further immunological testing. Acylation of Art v 1 gave derivatives (caaArt v 1 and citArt v 1) with about 80 % modified amino groups. The derivatives were in the monomeric form and had dramatically reduced pI values. Both derivatives were relatively stable at neutral pH values, while the acyl groups undergo hydrolysis under acidic conditions. Modification of allergens by cis-aconitylation and citraconylation could be a new tool for obtaining allergoids., Art v1 je glavni alergen polena crnog pelina (Artemisia vulgaris), značajnog uzročnika polenske groznice širom Evrope. Alergen-specifična imunoterapija je za sada jedini delotvoran način za tretiranje alergija, pri čemu primena modifikovanih alergena čini ovakav tretman bezbednijim i efikasnijim. U ovom radu, dva od tri (anhidrid cis-akonitne, citrakonske i 2,3-dimetilmaleinske kiseline) ispitivana anhidrida su se pokazala pogodnim za hemijske modifikacije alergena. Art v 1 je modifikovan cis-akonitilovanjem i citrakonilovanjem u cilju dobijanja derivata Art v 1 pogodnih za dalje imunološke testove. Acilovanjem Art v 1 dobijeni su derivati (caaArt v 1 i citArt v 1) sa oko 80 % izmodifikovanih amino grupa. Dobijeni derivati su monomerni, sa molekulskom masom sličnom nativnom Art v 1, ali sa dramatično smanjenim pI vrednostima. Oba derivata su relativno stabilna u neutralnoj, dok se u kiseloj sredini acil grupe hidrolizuju. Modifikacija alergena cis-akonitilovanjem i citrakonilovanjem može biti novi način za dobijanje alergoida.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation, Hemijske modifikacije Art v 1, glavnog alergena Artemisia vulgaris, cis-akonitilovanjem i citrakonilovanjem",
pages = "366-359",
number = "4",
volume = "74",
doi = "10.2298/JSC0904359S"
}

Stanić, D., Burazer, L., Gavrović-Jankulović, M., Jankov, R.,& Ćirković-Veličković, T.. (2009). Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 74(4), 359-366.
https://doi.org/10.2298/JSC0904359S

Stanić D, Burazer L, Gavrović-Jankulović M, Jankov R, Ćirković-Veličković T. Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation. in Journal of the Serbian Chemical Society. 2009;74(4):359-366.
doi:10.2298/JSC0904359S .

Stanić, Dragana, Burazer, Lidija, Gavrović-Jankulović, Marija, Jankov, Ratko, Ćirković-Veličković, Tanja, "Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation" in Journal of the Serbian Chemical Society, 74, no. 4 (2009):359-366,
https://doi.org/10.2298/JSC0904359S . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Pjanović, Rada V.
AU  - Burazer, Lidija
AU  - Velicković, Sava J.
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/269
AB  - BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system. (C) 2008 Society of Chemical Industry
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion
EP  - 14
IS  - 1
SP  - 8
VL  - 89
DO  - 10.1002/jsfa.3404
ER  - 

@article{
author = "Polović, Natalija and Pjanović, Rada V. and Burazer, Lidija and Velicković, Sava J. and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system. (C) 2008 Society of Chemical Industry",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion",
pages = "14-8",
number = "1",
volume = "89",
doi = "10.1002/jsfa.3404"
}

Polović, N., Pjanović, R. V., Burazer, L., Velicković, S. J., Jankov, R.,& Ćirković-Veličković, T.. (2009). Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 89(1), 8-14.
https://doi.org/10.1002/jsfa.3404

Polović N, Pjanović RV, Burazer L, Velicković SJ, Jankov R, Ćirković-Veličković T. Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture. 2009;89(1):8-14.
doi:10.1002/jsfa.3404 .

Polović, Natalija, Pjanović, Rada V., Burazer, Lidija, Velicković, Sava J., Jankov, Ratko, Ćirković-Veličković, Tanja, "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion" in Journal of the Science of Food and Agriculture, 89, no. 1 (2009):8-14,
https://doi.org/10.1002/jsfa.3404 . .

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  - Grozdanović, Milica
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/274
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen
EP  - 249
SP  - 249
VL  - 64
UR  - https://hdl.handle.net/21.15107/rcub_intor_274
ER  - 

@conference{
author = "Grozdanović, Milica and Burazer, Lidija and Vučković, Olga and Ćirković-Veličković, Tanja and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen",
pages = "249-249",
volume = "64",
url = "https://hdl.handle.net/21.15107/rcub_intor_274"
}

Grozdanović, M., Burazer, L., Vučković, O., Ćirković-Veličković, T., Jankov, R.,& Gavrović-Jankulović, M.. (2009). Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 249-249.
https://hdl.handle.net/21.15107/rcub_intor_274

Grozdanović M, Burazer L, Vučković O, Ćirković-Veličković T, Jankov R, Gavrović-Jankulović M. Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen. in Allergy. 2009;64:249-249.
https://hdl.handle.net/21.15107/rcub_intor_274 .

Grozdanović, Milica, Burazer, Lidija, Vučković, Olga, Ćirković-Veličković, Tanja, Jankov, Ratko, Gavrović-Jankulović, Marija, "Characterisation of a thaumatin-like homologue from birch (Betula verrucosa) pollen" in Allergy, 64 (2009):249-249,
https://hdl.handle.net/21.15107/rcub_intor_274 .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Spasic, Milena
AU  - Veličković, Tanja
AU  - Stojanović, Marijana
AU  - Inić-Kanada, Aleksandra
AU  - Dimitrijevic, Ljiliana
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Becker, Wolf-Meinhard
AU  - Jankov, Ratko
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/248
AB  - Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwifruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.
T2  - Molecular Nutrition and Food Research
T1  - Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA
EP  - 707
IS  - 6
SP  - 701
VL  - 52
DO  - 10.1002/mnfr.200700286
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Spasic, Milena and Veličković, Tanja and Stojanović, Marijana and Inić-Kanada, Aleksandra and Dimitrijevic, Ljiliana and Lindner, Buko and Petersen, Arnd and Becker, Wolf-Meinhard and Jankov, Ratko",
year = "2008",
abstract = "Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwifruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.",
journal = "Molecular Nutrition and Food Research",
title = "Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA",
pages = "707-701",
number = "6",
volume = "52",
doi = "10.1002/mnfr.200700286"
}

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

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

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

TY  - CONF
AU  - Polović, Natalija
AU  - Obradović, A.
AU  - Spasić, M.
AU  - Plećaš, Bosiljka
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/253
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - Transit times of kiwi fruit proteins through rat's gastrointestinal
EP  - 429
SP  - 428
VL  - 63
UR  - https://hdl.handle.net/21.15107/rcub_intor_253
ER  - 

@conference{
author = "Polović, Natalija and Obradović, A. and Spasić, M. and Plećaš, Bosiljka and Burazer, Lidija and Gavrović-Jankulović, Marija and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "Transit times of kiwi fruit proteins through rat's gastrointestinal",
pages = "429-428",
volume = "63",
url = "https://hdl.handle.net/21.15107/rcub_intor_253"
}

Polović, N., Obradović, A., Spasić, M., Plećaš, B., Burazer, L., Gavrović-Jankulović, M., Jankov, R.,& Ćirković-Veličković, T.. (2008). Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy
Blackwell Publishing, Oxford., 63, 428-429.
https://hdl.handle.net/21.15107/rcub_intor_253

Polović N, Obradović A, Spasić M, Plećaš B, Burazer L, Gavrović-Jankulović M, Jankov R, Ćirković-Veličković T. Transit times of kiwi fruit proteins through rat's gastrointestinal. in Allergy. 2008;63:428-429.
https://hdl.handle.net/21.15107/rcub_intor_253 .

Polović, Natalija, Obradović, A., Spasić, M., Plećaš, Bosiljka, Burazer, Lidija, Gavrović-Jankulović, Marija, Jankov, Ratko, Ćirković-Veličković, Tanja, "Transit times of kiwi fruit proteins through rat's gastrointestinal" in Allergy, 63 (2008):428-429,
https://hdl.handle.net/21.15107/rcub_intor_253 .

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  - CONF
AU  - Stanić, Dragana
AU  - Milovanović, Mina
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/254
PB  - Wiley-Blackwell, Malden
C3  - Allergy
T1  - Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation
EP  - 496
SP  - 496
VL  - 63
UR  - https://hdl.handle.net/21.15107/rcub_intor_254
ER  - 

@conference{
author = "Stanić, Dragana and Milovanović, Mina and Atanasković-Marković, Marina and Burazer, Lidija and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Wiley-Blackwell, Malden",
journal = "Allergy",
title = "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation",
pages = "496-496",
volume = "63",
url = "https://hdl.handle.net/21.15107/rcub_intor_254"
}

Stanić, D., Milovanović, M., Atanasković-Marković, M., Burazer, L., Jankov, R.,& Ćirković-Veličković, T.. (2008). Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy
Wiley-Blackwell, Malden., 63, 496-496.
https://hdl.handle.net/21.15107/rcub_intor_254

Stanić D, Milovanović M, Atanasković-Marković M, Burazer L, Jankov R, Ćirković-Veličković T. Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy. 2008;63:496-496.
https://hdl.handle.net/21.15107/rcub_intor_254 .

Stanić, Dragana, Milovanović, Mina, Atanasković-Marković, Marina, Burazer, Lidija, Jankov, Ratko, Ćirković-Veličković, Tanja, "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation" in Allergy, 63 (2008):496-496,
https://hdl.handle.net/21.15107/rcub_intor_254 .

TY  - JOUR
AU  - Polović, Natalija
AU  - Blanuša, Milan
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Veličković, Tanja
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/225
AB  - Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
EP  - 771
IS  - 5
SP  - 764
VL  - 37
DO  - 10.1111/j.1365-2222.2007.02703.x
ER  - 

@article{
author = "Polović, Natalija and Blanuša, Milan and Gavrović-Jankulović, Marija and Atanasković-Marković, Marina and Burazer, Lidija and Jankov, Ratko and Veličković, Tanja",
year = "2007",
abstract = "Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.",
journal = "Clinical and Experimental Allergy",
title = "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro",
pages = "771-764",
number = "5",
volume = "37",
doi = "10.1111/j.1365-2222.2007.02703.x"
}

Polović, N., Blanuša, M., Gavrović-Jankulović, M., Atanasković-Marković, M., Burazer, L., Jankov, R.,& Veličković, T.. (2007). A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy, 37(5), 764-771.
https://doi.org/10.1111/j.1365-2222.2007.02703.x

Polović N, Blanuša M, Gavrović-Jankulović M, Atanasković-Marković M, Burazer L, Jankov R, Veličković T. A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy. 2007;37(5):764-771.
doi:10.1111/j.1365-2222.2007.02703.x .

Polović, Natalija, Blanuša, Milan, Gavrović-Jankulović, Marija, Atanasković-Marković, Marina, Burazer, Lidija, Jankov, Ratko, Veličković, Tanja, "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro" in Clinical and Experimental Allergy, 37, no. 5 (2007):764-771,
https://doi.org/10.1111/j.1365-2222.2007.02703.x . .

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 . .

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Polović, Natalija
AU  - Gavrović-Jankulović, Marija
AU  - Burazer, Lidija
AU  - Đergović-Petrović, Danica
AU  - Vučković, Olga
AU  - Drobnjak, Olika
AU  - Šporčić, Zorica
AU  - Atanasković-Marković, Marina
AU  - Jankov, Ratko
PY  - 2006
UR  - http://intor.torlakinstitut.com/handle/123456789/220
AB  - Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones.
AB  - U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract
T1  - Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta
EP  - 888
IS  - 8-9
SP  - 879
VL  - 71
DO  - 10.2298/JSC0609879C
ER  - 

@article{
author = "Ćirković-Veličković, Tanja and Polović, Natalija and Gavrović-Jankulović, Marija and Burazer, Lidija and Đergović-Petrović, Danica and Vučković, Olga and Drobnjak, Olika and Šporčić, Zorica and Atanasković-Marković, Marina and Jankov, Ratko",
year = "2006",
abstract = "Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones., U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract, Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta",
pages = "888-879",
number = "8-9",
volume = "71",
doi = "10.2298/JSC0609879C"
}

Ćirković-Veličković, T., Polović, N., Gavrović-Jankulović, M., Burazer, L., Đergović-Petrović, D., Vučković, O., Drobnjak, O., Šporčić, Z., Atanasković-Marković, M.,& Jankov, R.. (2006). Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 71(8-9), 879-888.
https://doi.org/10.2298/JSC0609879C

Ćirković-Veličković T, Polović N, Gavrović-Jankulović M, Burazer L, Đergović-Petrović D, Vučković O, Drobnjak O, Šporčić Z, Atanasković-Marković M, Jankov R. Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society. 2006;71(8-9):879-888.
doi:10.2298/JSC0609879C .

Ćirković-Veličković, Tanja, Polović, Natalija, Gavrović-Jankulović, Marija, Burazer, Lidija, Đergović-Petrović, Danica, Vučković, Olga, Drobnjak, Olika, Šporčić, Zorica, Atanasković-Marković, Marina, Jankov, Ratko, "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract" in Journal of the Serbian Chemical Society, 71, no. 8-9 (2006):879-888,
https://doi.org/10.2298/JSC0609879C . .

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
AU  - Prisić, S.
AU  - Jankov, Ratko
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
PY  - 2005
UR  - http://intor.torlakinstitut.com/handle/123456789/201
AB  - Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Food and Agricultural Immunology
T1  - Allergenic potency of kiwi fruit during fruit development
EP  - 128
IS  - 2
SP  - 117
VL  - 16
DO  - 10.1080/09540100500090804
ER  - 

@article{
author = "Gavrović-Jankulović, Marija and Polović, Natalija and Prisić, S. and Jankov, Ratko and Atanasković-Marković, Marina and Vučković, Olga and Ćirković-Veličković, Tanja",
year = "2005",
abstract = "Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Food and Agricultural Immunology",
title = "Allergenic potency of kiwi fruit during fruit development",
pages = "128-117",
number = "2",
volume = "16",
doi = "10.1080/09540100500090804"
}

Gavrović-Jankulović, M., Polović, N., Prisić, S., Jankov, R., Atanasković-Marković, M., Vučković, O.,& Ćirković-Veličković, T.. (2005). Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology
Taylor & Francis Ltd, Abingdon., 16(2), 117-128.
https://doi.org/10.1080/09540100500090804

Gavrović-Jankulović M, Polović N, Prisić S, Jankov R, Atanasković-Marković M, Vučković O, Ćirković-Veličković T. Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology. 2005;16(2):117-128.
doi:10.1080/09540100500090804 .

Gavrović-Jankulović, Marija, Polović, Natalija, Prisić, S., Jankov, Ratko, Atanasković-Marković, Marina, Vučković, Olga, Ćirković-Veličković, Tanja, "Allergenic potency of kiwi fruit during fruit development" in Food and Agricultural Immunology, 16, no. 2 (2005):117-128,
https://doi.org/10.1080/09540100500090804 . .

TY  - JOUR
AU  - Šeatović, Saša S.
AU  - Inić-Kanada, Aleksandra
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Jankov, Ratko
AU  - Dimitrijević, Ljiljana
PY  - 2004
UR  - http://intor.torlakinstitut.com/handle/123456789/181
AB  - According to the recommendation of the World Health Organization (WHO), the use of an in vivo test for measuring of the potency of tetanus toxoid vaccine (TTdV) is still unavoidable, but the establishment of a convenient in vitro test would significantly improve the work in this field. A sandwich enzyme-linked immunosorbent assay (sELISA) was developed for a rapid and sensitive quantification of tetanus toxoid (TTd). We produced four monoclonal antibodies (MAbs) designated 41, 51, 62, and 71 that reacted with TTd and recognized, different antigenic determinants on TTd. We also used two of these antibodies for developing a sELISA, with MoAb 71 as an immobilized and MoAb 51 as a capture antibody. The measurement range of this assay was from 31-1000 ng/mL and the minimum detection limit for TTd was 31 ng/mL. This high sensitivity of this sELISA and its good reproducibility suggest that the developed method could be reliably used to estimate the concentration of TTd, which could be easily extrapolated to the estimation of vaccine potency.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Journal of Immunoassay & Immunochemistry
T1  - Development of sandwich enzyme-linked immunosorbent assay for determination of tetanus toxoid concentration
EP  - 44
IS  - 1
SP  - 31
VL  - 25
DO  - 10.1081/IAS-120027224
ER  - 

@article{
author = "Šeatović, Saša S. and Inić-Kanada, Aleksandra and Stojanović, Marijana and Živković, Irena and Jankov, Ratko and Dimitrijević, Ljiljana",
year = "2004",
abstract = "According to the recommendation of the World Health Organization (WHO), the use of an in vivo test for measuring of the potency of tetanus toxoid vaccine (TTdV) is still unavoidable, but the establishment of a convenient in vitro test would significantly improve the work in this field. A sandwich enzyme-linked immunosorbent assay (sELISA) was developed for a rapid and sensitive quantification of tetanus toxoid (TTd). We produced four monoclonal antibodies (MAbs) designated 41, 51, 62, and 71 that reacted with TTd and recognized, different antigenic determinants on TTd. We also used two of these antibodies for developing a sELISA, with MoAb 71 as an immobilized and MoAb 51 as a capture antibody. The measurement range of this assay was from 31-1000 ng/mL and the minimum detection limit for TTd was 31 ng/mL. This high sensitivity of this sELISA and its good reproducibility suggest that the developed method could be reliably used to estimate the concentration of TTd, which could be easily extrapolated to the estimation of vaccine potency.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Journal of Immunoassay & Immunochemistry",
title = "Development of sandwich enzyme-linked immunosorbent assay for determination of tetanus toxoid concentration",
pages = "44-31",
number = "1",
volume = "25",
doi = "10.1081/IAS-120027224"
}

Šeatović, S. S., Inić-Kanada, A., Stojanović, M., Živković, I., Jankov, R.,& Dimitrijević, L.. (2004). Development of sandwich enzyme-linked immunosorbent assay for determination of tetanus toxoid concentration. in Journal of Immunoassay & Immunochemistry
Taylor & Francis Inc, Philadelphia., 25(1), 31-44.
https://doi.org/10.1081/IAS-120027224

Šeatović SS, Inić-Kanada A, Stojanović M, Živković I, Jankov R, Dimitrijević L. Development of sandwich enzyme-linked immunosorbent assay for determination of tetanus toxoid concentration. in Journal of Immunoassay & Immunochemistry. 2004;25(1):31-44.
doi:10.1081/IAS-120027224 .

Šeatović, Saša S., Inić-Kanada, Aleksandra, Stojanović, Marijana, Živković, Irena, Jankov, Ratko, Dimitrijević, Ljiljana, "Development of sandwich enzyme-linked immunosorbent assay for determination of tetanus toxoid concentration" in Journal of Immunoassay & Immunochemistry, 25, no. 1 (2004):31-44,
https://doi.org/10.1081/IAS-120027224 . .

TY  - JOUR
AU  - Polović, Natalija
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Burazer, Lidija
AU  - Đergović-Petrović, Danica
AU  - Vučković, Olga
AU  - Jankov, Ratko
PY  - 2004
UR  - http://intor.torlakinstitut.com/handle/123456789/184
AB  - This study considers the influence of exposure to simulated gastrointestinal conditions (saliva, gut, intestine and acidic conditions of the gut) on IgG binding of unmodified allergens and three types of LMW allergoids of Artemisia vulgaris pollen extract obtained by means of potassium cyanate succinic and maleic anhydride. It also concerns the optimization of a self-developed ELISA assay for comparison of the specific IgG binding of mugwort pollen extract and modified mugwort pollen derivatives. The ELISA was conducted with a mugwort pollen extract coupled to the plate, using the sera from 12 mugwort- pollen allergic patients. The exposure to saliva fluid for 2 min did not influence the IgG binding properties of allergens and allergoids. Exposure of mugwort pollen allergens and LMW allergoids to the acidic conditions of the gut did not dramatically change their IgG binding properties. By exposing mugwort pollen extract and LMW derivatives to the SGF conditions for 1 h, the percent of IgG binding epitopes was reduced to a half of its starting value in the extract and to about 30%in all the allergoid samples. After prolonged exposure only the carbamyl derivative showed reduced IgG binding. Changes of the IgG binding potential of all four samples after exposure in SIF followed a similar pattern.
AB  - Predmet ovog rada je ispitivanje promena IgG vezivanja nemodifikovanih alergena polena A. vulgaris i tri tipa alergoida malih molekulskih masa dobijenih tretmanom sa kalijum-cijanatom, i anhidridima ćilibarne i meleinske posle izlaganja uslovima gastrointestinalnog trakta (saliva, želudac, tanko crevo i kisela sredina želudačnog soka) i optimizacija domaćeg ELISA testa za određivanje IgG vezivanja alergena i alergoida polena pelina.UELISA testu je za pločicu kuplovan ekstrakt polena pelina i korišćeni su serumi 12 pacijenata alergičnih na pelin. Izlaganje salivi u trajanju od 2 minuta ne utiče na IgG vezujuće osobine alergena i alergoida. Izlaganje kiseloj sredini želudačnog soka značajno ne utiče na IgG vezujuće osobine alergena i alergoida polena pelina. Posle izlaganja simuliranom želudačnom soku alergena i derivata u trajanju od 1 sata, procenat IgG vezujućih epitopa u nemodifikovanom uzorku se smanjuje na polovinu početne vrednosti i na oko 30 % kod sva tri derivata. Jedino se kod karbamil-derivata % IgG vezivanja dodatno smanjuje sa produžavanjem izlaganja SGF-u.Promene u IgG vezujućem potencijalu sva 4 uzorka posle izlaganja simuliranim uslovima tankog creva prate sličan obrazac.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest
T1  - Igg vezivanje alergena i alergoida polena pelina prethodno izloženih simuliranim uslovima gastrointestinalnog trakta mereno domaćim elisa testom
EP  - 540
IS  - 7
SP  - 533
VL  - 69
DO  - 10.2298/JSC0407533P
ER  - 

@article{
author = "Polović, Natalija and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Burazer, Lidija and Đergović-Petrović, Danica and Vučković, Olga and Jankov, Ratko",
year = "2004",
abstract = "This study considers the influence of exposure to simulated gastrointestinal conditions (saliva, gut, intestine and acidic conditions of the gut) on IgG binding of unmodified allergens and three types of LMW allergoids of Artemisia vulgaris pollen extract obtained by means of potassium cyanate succinic and maleic anhydride. It also concerns the optimization of a self-developed ELISA assay for comparison of the specific IgG binding of mugwort pollen extract and modified mugwort pollen derivatives. The ELISA was conducted with a mugwort pollen extract coupled to the plate, using the sera from 12 mugwort- pollen allergic patients. The exposure to saliva fluid for 2 min did not influence the IgG binding properties of allergens and allergoids. Exposure of mugwort pollen allergens and LMW allergoids to the acidic conditions of the gut did not dramatically change their IgG binding properties. By exposing mugwort pollen extract and LMW derivatives to the SGF conditions for 1 h, the percent of IgG binding epitopes was reduced to a half of its starting value in the extract and to about 30%in all the allergoid samples. After prolonged exposure only the carbamyl derivative showed reduced IgG binding. Changes of the IgG binding potential of all four samples after exposure in SIF followed a similar pattern., Predmet ovog rada je ispitivanje promena IgG vezivanja nemodifikovanih alergena polena A. vulgaris i tri tipa alergoida malih molekulskih masa dobijenih tretmanom sa kalijum-cijanatom, i anhidridima ćilibarne i meleinske posle izlaganja uslovima gastrointestinalnog trakta (saliva, želudac, tanko crevo i kisela sredina želudačnog soka) i optimizacija domaćeg ELISA testa za određivanje IgG vezivanja alergena i alergoida polena pelina.UELISA testu je za pločicu kuplovan ekstrakt polena pelina i korišćeni su serumi 12 pacijenata alergičnih na pelin. Izlaganje salivi u trajanju od 2 minuta ne utiče na IgG vezujuće osobine alergena i alergoida. Izlaganje kiseloj sredini želudačnog soka značajno ne utiče na IgG vezujuće osobine alergena i alergoida polena pelina. Posle izlaganja simuliranom želudačnom soku alergena i derivata u trajanju od 1 sata, procenat IgG vezujućih epitopa u nemodifikovanom uzorku se smanjuje na polovinu početne vrednosti i na oko 30 % kod sva tri derivata. Jedino se kod karbamil-derivata % IgG vezivanja dodatno smanjuje sa produžavanjem izlaganja SGF-u.Promene u IgG vezujućem potencijalu sva 4 uzorka posle izlaganja simuliranim uslovima tankog creva prate sličan obrazac.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest, Igg vezivanje alergena i alergoida polena pelina prethodno izloženih simuliranim uslovima gastrointestinalnog trakta mereno domaćim elisa testom",
pages = "540-533",
number = "7",
volume = "69",
doi = "10.2298/JSC0407533P"
}

Polović, N., Ćirković-Veličković, T., Gavrović-Jankulović, M., Burazer, L., Đergović-Petrović, D., Vučković, O.,& Jankov, R.. (2004). IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 69(7), 533-540.
https://doi.org/10.2298/JSC0407533P

Polović N, Ćirković-Veličković T, Gavrović-Jankulović M, Burazer L, Đergović-Petrović D, Vučković O, Jankov R. IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest. in Journal of the Serbian Chemical Society. 2004;69(7):533-540.
doi:10.2298/JSC0407533P .

Polović, Natalija, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Burazer, Lidija, Đergović-Petrović, Danica, Vučković, Olga, Jankov, Ratko, "IgG binding of mugwort pollen allergens and allergoids exposed to simulated gastrointestinal conditions measured by a self-developed ELISAtest" in Journal of the Serbian Chemical Society, 69, no. 7 (2004):533-540,
https://doi.org/10.2298/JSC0407533P . .

TY  - JOUR
AU  - Inić-Kanada, Aleksandra
AU  - Stojanović, Marijana
AU  - Šeatović, Saša S.
AU  - Živković, Irena
AU  - Jankov, Ratko
AU  - Živančević-Simonović, Snežana
AU  - Dimitrijević, Ljiljana
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/154
AB  - Monoclonal antibodies (MoAb) are usually produced as the secretion products of cloned B lymphoblastoid cell lines. Advantages of MoAbs are that they could be selected to have desired specificity and produced in relatively large quantities of consistent quality and char acteristics. Interest in the production of re agents specific for human kappa (K) chain can be explained by the fact that many pathological conditions are accompanied by frequency of immunoglobulins with K light chain. The aim of this study was production of stable MoAb-se creating hybridoma with ability to secrete imunoglobulin specific for human K chain, immunochemical characterization of this MoAb and its possible application. Murine monoclonal antibody, as signed as MoAt 44, produced by hybridoma technology is specific for human kappa chain and fully immunochemically characterized. In this paper, we reported that MoAb 44 demonstrated excellent properties in most immunochemical techniques (immunoblot, dot-blot, immunofluorescence, double and radial immunodiffusion, immunoelectrophoresis...), which highly recommend this MoAb for the application as a tool for re search and immunodiagnostics.
AB  - Monoklonska antitela (MoAt) su sekretorni proizvodi kloniranih B ćelijskih limfoblastoidnih linija. Od poliklonskih antitela ih razlikuje: definisana specifičnost vezivanja, homogenost i mogućnost proizvodnje u velikoj količini. Budući da su brojna patološka stanja povezana sa sekrecijom imunoglobulina u čijem sastavu se nalazi kapa (k) tip lakog lanca, proizvodnja specifičnih monoklonskih antitela našla bi svoje mesto u njihovoj dijagnostici. Stoga je cilj našeg rada bio dobijanje stabilnog mišjeg hibridomskog klona koji bi sekretovao MoAt specifično za humani k lanac, imunohemijska karakterizacija tog MoAt i ispitivanje mogućnosti njegove primene. Mišje monoklonsko antitelo, označeno kao MoAt 44, proizvedeno hibridomskom tehnologijom, specifično je za k lanac humanih imunoglobulina i u potpunosti imunohemijski okarakterisano. MoAt 44 može da se koristi u većini imunohemijskih tehnika (imunoblot-u, dot-blot-u, imunofluorescenci, dvostrukoj i radijalnoj imunodifuziji, imunoelektroforezi...), što omogućava njegovu primenu u naučno-istraživačkom radu i imunodijagnostici.
PB  - Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac
T2  - Medicus
T1  - The murine monoclonal antibody specific for human kappa immunoglobuline chain and its application possibilities
T1  - Mišje monoklonsko antitelo specifično za kapa lanac humanih imunoglobulina i mogućnosti njegove primene
EP  - 25
IS  - 1
SP  - 21
VL  - 3
UR  - https://hdl.handle.net/21.15107/rcub_intor_154
ER  - 

@article{
author = "Inić-Kanada, Aleksandra and Stojanović, Marijana and Šeatović, Saša S. and Živković, Irena and Jankov, Ratko and Živančević-Simonović, Snežana and Dimitrijević, Ljiljana",
year = "2002",
abstract = "Monoclonal antibodies (MoAb) are usually produced as the secretion products of cloned B lymphoblastoid cell lines. Advantages of MoAbs are that they could be selected to have desired specificity and produced in relatively large quantities of consistent quality and char acteristics. Interest in the production of re agents specific for human kappa (K) chain can be explained by the fact that many pathological conditions are accompanied by frequency of immunoglobulins with K light chain. The aim of this study was production of stable MoAb-se creating hybridoma with ability to secrete imunoglobulin specific for human K chain, immunochemical characterization of this MoAb and its possible application. Murine monoclonal antibody, as signed as MoAt 44, produced by hybridoma technology is specific for human kappa chain and fully immunochemically characterized. In this paper, we reported that MoAb 44 demonstrated excellent properties in most immunochemical techniques (immunoblot, dot-blot, immunofluorescence, double and radial immunodiffusion, immunoelectrophoresis...), which highly recommend this MoAb for the application as a tool for re search and immunodiagnostics., Monoklonska antitela (MoAt) su sekretorni proizvodi kloniranih B ćelijskih limfoblastoidnih linija. Od poliklonskih antitela ih razlikuje: definisana specifičnost vezivanja, homogenost i mogućnost proizvodnje u velikoj količini. Budući da su brojna patološka stanja povezana sa sekrecijom imunoglobulina u čijem sastavu se nalazi kapa (k) tip lakog lanca, proizvodnja specifičnih monoklonskih antitela našla bi svoje mesto u njihovoj dijagnostici. Stoga je cilj našeg rada bio dobijanje stabilnog mišjeg hibridomskog klona koji bi sekretovao MoAt specifično za humani k lanac, imunohemijska karakterizacija tog MoAt i ispitivanje mogućnosti njegove primene. Mišje monoklonsko antitelo, označeno kao MoAt 44, proizvedeno hibridomskom tehnologijom, specifično je za k lanac humanih imunoglobulina i u potpunosti imunohemijski okarakterisano. MoAt 44 može da se koristi u većini imunohemijskih tehnika (imunoblot-u, dot-blot-u, imunofluorescenci, dvostrukoj i radijalnoj imunodifuziji, imunoelektroforezi...), što omogućava njegovu primenu u naučno-istraživačkom radu i imunodijagnostici.",
publisher = "Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac",
journal = "Medicus",
title = "The murine monoclonal antibody specific for human kappa immunoglobuline chain and its application possibilities, Mišje monoklonsko antitelo specifično za kapa lanac humanih imunoglobulina i mogućnosti njegove primene",
pages = "25-21",
number = "1",
volume = "3",
url = "https://hdl.handle.net/21.15107/rcub_intor_154"
}

Inić-Kanada, A., Stojanović, M., Šeatović, S. S., Živković, I., Jankov, R., Živančević-Simonović, S.,& Dimitrijević, L.. (2002). The murine monoclonal antibody specific for human kappa immunoglobuline chain and its application possibilities. in Medicus
Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac., 3(1), 21-25.
https://hdl.handle.net/21.15107/rcub_intor_154

Inić-Kanada A, Stojanović M, Šeatović SS, Živković I, Jankov R, Živančević-Simonović S, Dimitrijević L. The murine monoclonal antibody specific for human kappa immunoglobuline chain and its application possibilities. in Medicus. 2002;3(1):21-25.
https://hdl.handle.net/21.15107/rcub_intor_154 .

Inić-Kanada, Aleksandra, Stojanović, Marijana, Šeatović, Saša S., Živković, Irena, Jankov, Ratko, Živančević-Simonović, Snežana, Dimitrijević, Ljiljana, "The murine monoclonal antibody specific for human kappa immunoglobuline chain and its application possibilities" in Medicus, 3, no. 1 (2002):21-25,
https://hdl.handle.net/21.15107/rcub_intor_154 .

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Bukilica, Mirjana
AU  - Mandić, Ljuba M.
AU  - Petrović, Spomenka
AU  - Jankov, Ratko
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/140
AB  - An acid phosphatase from an extract of mugwort (Artemisia vulgaris) pollen was purified by a factor of 48 by a combination of ion exchange and gel-chromatography. The molecular weights of the enzyme were 76 kDa and 73 kDa, determined by gel filtration on a Sephadex G-100 sf column and by SDS PAGE(under reducing and non-reducing conditions), respectively. In analytical isoelectrofocusing, the enzyme appears as two very close bands pI at about 4.2. The optimum pH for the enzyme is 5.4. The apparent Km for p-nitrophenyl phosphate was estimated to be 0.16mM. The purified enzyme has broad specificity, and hydrolyses p-nitrophenyl phosphate and α-naphthyl phosphate. Pyrophosphate and O-phospho-L-tyrosine were estimated to be the best substrates for this enzyme as potential in vivo substrates. The enzyme is inhibited competitively by phosphate (Ki = 1.25 mM), molybdate (Ki = 0.055 mM) and pyrophosphate (Ki = 6.7 mM) and non-competitively by fluoride (Ki = 9.8 mM). Metal ions such as Hg2+, Cu2+ and Zn2+ express an inhibitory effect on the enzyme, while the enzyme is slightly activated by non-ionic detergents, Tween 20 and Triton X-100. There is no change in the enzyme activity in the presence of tartrate, citrate, EDTA, 1,10-phenanthroline and sulfhydryl-group modifiers such as p-chloromercuribenzoate and N-ethylmaleimide.
AB  - Kisela fosfataza ekstrakta polena visokog korova (Artemisia vulgaris) je prečišćena 48 puta kombinacijom jonoizmenjivačke i gel-hromatografije. Molekulska težina enzima je 76 kDa i 73 kDa, određena gel-filtracijom na matriksu Sephadex G-100 sf i SDS PAG elektroforezom (pri redukujućim i neredukujućim uslovima), respektivno. Pri izoelektrofokusiranju, enzim se sastoji iz dve vrlo bliske trake pI vrednosti oko 4,2. Optimalno pH za aktivnost enzima je 5,4. PrividnoKmza hidrolizu p-nitrofenil-fosfata je procenjeno da je 0,16 mM. Prečišćeni enzim ima široku specifičnost hidrolizuje p-nitrofenil-fosfat i α-naftil-fosfat. Pirofosfat i O-fosfo-L-tirozin su procenjeni kao najbolji od potencijalnih in vivo supstrata ovog enzima. Enzim je inhibiran kompetitivno fosfatom (Ki=1,25 mM), molibdatom (Ki=0,055 mM) i pirofosfatom (Ki=6,7 mM) a nekompetitivno fluoridom (Ki= 9,8mM). Joni metala, kao što su Hg2+, Cu2+ i Zn2+ iskazuju inhibitorni efekat na enzim, dok je efekat ne-jonskih detergenata, kao što su Tween 20 i Triton X-100 blago aktivirajuć i. Nema promene u aktivnosti enzima u prisustvu tartarata, citrata, EDTA 1,10-fenantrolina i modifikatora sulfhidrilnih grupa kao što su p-hloromerkuribenzoat i N-etilmaleimid.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract
T1  - Izolovanje i delimična karakterizacija kisele fosfataze ekstrakta polena Artemisia vulgaris
EP  - 572
IS  - 8-9
SP  - 567
VL  - 67
UR  - https://hdl.handle.net/21.15107/rcub_intor_140
ER  - 

@article{
author = "Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Bukilica, Mirjana and Mandić, Ljuba M. and Petrović, Spomenka and Jankov, Ratko",
year = "2002",
abstract = "An acid phosphatase from an extract of mugwort (Artemisia vulgaris) pollen was purified by a factor of 48 by a combination of ion exchange and gel-chromatography. The molecular weights of the enzyme were 76 kDa and 73 kDa, determined by gel filtration on a Sephadex G-100 sf column and by SDS PAGE(under reducing and non-reducing conditions), respectively. In analytical isoelectrofocusing, the enzyme appears as two very close bands pI at about 4.2. The optimum pH for the enzyme is 5.4. The apparent Km for p-nitrophenyl phosphate was estimated to be 0.16mM. The purified enzyme has broad specificity, and hydrolyses p-nitrophenyl phosphate and α-naphthyl phosphate. Pyrophosphate and O-phospho-L-tyrosine were estimated to be the best substrates for this enzyme as potential in vivo substrates. The enzyme is inhibited competitively by phosphate (Ki = 1.25 mM), molybdate (Ki = 0.055 mM) and pyrophosphate (Ki = 6.7 mM) and non-competitively by fluoride (Ki = 9.8 mM). Metal ions such as Hg2+, Cu2+ and Zn2+ express an inhibitory effect on the enzyme, while the enzyme is slightly activated by non-ionic detergents, Tween 20 and Triton X-100. There is no change in the enzyme activity in the presence of tartrate, citrate, EDTA, 1,10-phenanthroline and sulfhydryl-group modifiers such as p-chloromercuribenzoate and N-ethylmaleimide., Kisela fosfataza ekstrakta polena visokog korova (Artemisia vulgaris) je prečišćena 48 puta kombinacijom jonoizmenjivačke i gel-hromatografije. Molekulska težina enzima je 76 kDa i 73 kDa, određena gel-filtracijom na matriksu Sephadex G-100 sf i SDS PAG elektroforezom (pri redukujućim i neredukujućim uslovima), respektivno. Pri izoelektrofokusiranju, enzim se sastoji iz dve vrlo bliske trake pI vrednosti oko 4,2. Optimalno pH za aktivnost enzima je 5,4. PrividnoKmza hidrolizu p-nitrofenil-fosfata je procenjeno da je 0,16 mM. Prečišćeni enzim ima široku specifičnost hidrolizuje p-nitrofenil-fosfat i α-naftil-fosfat. Pirofosfat i O-fosfo-L-tirozin su procenjeni kao najbolji od potencijalnih in vivo supstrata ovog enzima. Enzim je inhibiran kompetitivno fosfatom (Ki=1,25 mM), molibdatom (Ki=0,055 mM) i pirofosfatom (Ki=6,7 mM) a nekompetitivno fluoridom (Ki= 9,8mM). Joni metala, kao što su Hg2+, Cu2+ i Zn2+ iskazuju inhibitorni efekat na enzim, dok je efekat ne-jonskih detergenata, kao što su Tween 20 i Triton X-100 blago aktivirajuć i. Nema promene u aktivnosti enzima u prisustvu tartarata, citrata, EDTA 1,10-fenantrolina i modifikatora sulfhidrilnih grupa kao što su p-hloromerkuribenzoat i N-etilmaleimid.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract, Izolovanje i delimična karakterizacija kisele fosfataze ekstrakta polena Artemisia vulgaris",
pages = "572-567",
number = "8-9",
volume = "67",
url = "https://hdl.handle.net/21.15107/rcub_intor_140"
}

Ćirković-Veličković, T., Gavrović-Jankulović, M., Bukilica, M., Mandić, L. M., Petrović, S.,& Jankov, R.. (2002). Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 67(8-9), 567-572.
https://hdl.handle.net/21.15107/rcub_intor_140

Ćirković-Veličković T, Gavrović-Jankulović M, Bukilica M, Mandić LM, Petrović S, Jankov R. Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract. in Journal of the Serbian Chemical Society. 2002;67(8-9):567-572.
https://hdl.handle.net/21.15107/rcub_intor_140 .

Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Bukilica, Mirjana, Mandić, Ljuba M., Petrović, Spomenka, Jankov, Ratko, "Isolation and partial characterization of an acid phosphatase from Artemisia vulgaris pollen extract" in Journal of the Serbian Chemical Society, 67, no. 8-9 (2002):567-572,
https://hdl.handle.net/21.15107/rcub_intor_140 .

TY  - JOUR
AU  - Ćirković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Prisić, S.
AU  - Jankov, Ratko
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Šporčić, Zorica
AU  - Paranos, Svetlana
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/151
AB  - Background: Reaction of epsilon-amino groups of lysine with potassium cyanate, maleic, or succinic anhydride leads to allergoids of low molecular weight. No study has been performed to compare their properties and investigate the influence of a residual group on allergenicity and human IgE- and IgG-binding of these derivatives. Methods: Allergoids of a pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, and succinic and maleic anhydride. Biochemical properties were investigated by determination of amino groups, enzyme activity, isoelectric focusing IEF and SDS-PAGE. IgE- and IgG-binding was determined using immunoblots and ELISA inhibition. Allergenicity was investigated by skin prick tests (SPT) on a group of 52 patients, of which 6 were control subjects, 30 were patients with no previous immunotherapy (IT), and 16 were patients undergoing immunotherapy. Results: The same degree of amino-group modification (more than 85%), residual enzyme activity (less then 15%), IEF, and SDS-PAGE pattern were noted. In the immunoblots of IgE-binding, there was more pronounced reduction in the succinyl and maleyl derivatives than in the carbamyl one. IgG-binding was less affected by carbamylation than by acid anhydride modification. The SPT showed that the succinylated derivative had the most reduced allergenicity (98% showed a reduced wheal diameter when tested with the succinyl derivative, 87% with the maleyl allergoid, and 83% with the carbamyl allergoid). The most significant difference among allergoids could be seen in the group of patients with high skin reactivity (83% of patients showed no reaction to the succinyl derivative when compared to the value of 28% for the carbamyl derivative or 22% for the maleyl derivative). Conclusions: According to our results, all three modification procedures yielded allergoids with a similar extent of modification. No single biochemical parameter investigated in the study could predict the degree of reduced allergenicity in vivo. The most reduced allergenicity was seen in the succinyl derivative while the preservation of IgG binding epitopes was of the highest degree for the carbamyl derivative.
PB  - Wiley, Hoboken
T2  - Allergy
T1  - The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties
EP  - 1020
IS  - 11
SP  - 1013
VL  - 57
DO  - 10.1034/j.1398-9995.2002.23739.x
ER  - 

@article{
author = "Ćirković, Tanja and Gavrović-Jankulović, Marija and Prisić, S. and Jankov, Ratko and Burazer, Lidija and Vučković, Olga and Šporčić, Zorica and Paranos, Svetlana",
year = "2002",
abstract = "Background: Reaction of epsilon-amino groups of lysine with potassium cyanate, maleic, or succinic anhydride leads to allergoids of low molecular weight. No study has been performed to compare their properties and investigate the influence of a residual group on allergenicity and human IgE- and IgG-binding of these derivatives. Methods: Allergoids of a pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, and succinic and maleic anhydride. Biochemical properties were investigated by determination of amino groups, enzyme activity, isoelectric focusing IEF and SDS-PAGE. IgE- and IgG-binding was determined using immunoblots and ELISA inhibition. Allergenicity was investigated by skin prick tests (SPT) on a group of 52 patients, of which 6 were control subjects, 30 were patients with no previous immunotherapy (IT), and 16 were patients undergoing immunotherapy. Results: The same degree of amino-group modification (more than 85%), residual enzyme activity (less then 15%), IEF, and SDS-PAGE pattern were noted. In the immunoblots of IgE-binding, there was more pronounced reduction in the succinyl and maleyl derivatives than in the carbamyl one. IgG-binding was less affected by carbamylation than by acid anhydride modification. The SPT showed that the succinylated derivative had the most reduced allergenicity (98% showed a reduced wheal diameter when tested with the succinyl derivative, 87% with the maleyl allergoid, and 83% with the carbamyl allergoid). The most significant difference among allergoids could be seen in the group of patients with high skin reactivity (83% of patients showed no reaction to the succinyl derivative when compared to the value of 28% for the carbamyl derivative or 22% for the maleyl derivative). Conclusions: According to our results, all three modification procedures yielded allergoids with a similar extent of modification. No single biochemical parameter investigated in the study could predict the degree of reduced allergenicity in vivo. The most reduced allergenicity was seen in the succinyl derivative while the preservation of IgG binding epitopes was of the highest degree for the carbamyl derivative.",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties",
pages = "1020-1013",
number = "11",
volume = "57",
doi = "10.1034/j.1398-9995.2002.23739.x"
}

Ćirković, T., Gavrović-Jankulović, M., Prisić, S., Jankov, R., Burazer, L., Vučković, O., Šporčić, Z.,& Paranos, S.. (2002). The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties. in Allergy
Wiley, Hoboken., 57(11), 1013-1020.
https://doi.org/10.1034/j.1398-9995.2002.23739.x

Ćirković T, Gavrović-Jankulović M, Prisić S, Jankov R, Burazer L, Vučković O, Šporčić Z, Paranos S. The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties. in Allergy. 2002;57(11):1013-1020.
doi:10.1034/j.1398-9995.2002.23739.x .

Ćirković, Tanja, Gavrović-Jankulović, Marija, Prisić, S., Jankov, Ratko, Burazer, Lidija, Vučković, Olga, Šporčić, Zorica, Paranos, Svetlana, "The influence of a residual group in low-molecular-weight allergoids of Artemisia vulgaris pollen on their allergenicity, IgE- and IgG-binding properties" in Allergy, 57, no. 11 (2002):1013-1020,
https://doi.org/10.1034/j.1398-9995.2002.23739.x . .

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

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

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

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

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