Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima

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Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (en)
Испитивање структуре и функције биолошки важних макромолекула у физиолошким и патолошким стањима (sr)
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (sr_RS)
Authors

Publications

Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice

Živković, Irena; Stojanović, Marijana; Petrušić, Vladimir; Inić-Kanada, Aleksandra; Dimitrijević, Ljiljana

(Wiley-Blackwell, Hoboken, 2011)

TY  - JOUR
AU  - Živković, Irena
AU  - Stojanović, Marijana
AU  - Petrušić, Vladimir
AU  - Inić-Kanada, Aleksandra
AU  - Dimitrijević, Ljiljana
PY  - 2011
UR  - http://intor.torlakinstitut.com/handle/123456789/321
AB  - Problem The antiphospholipid syndrome (APS) is a systemic autoimmune disease characterized by vascular thrombosis and/or pregnancy complications (lower fecundity and lower litter size), as well as by an increase in anti-beta(2) glycoprotein I (beta(2)GPI)-specific autoantibody titer. We have investigated how the genetic background of the immune system [T helper (Th) prevalence] and the type of animal model of APS influence the induced pathology. Method of Study Antiphospholipid syndrome induced by tetanus toxoid (TTd) hyper-immunization and by intravenous application of monoclonal anti-beta(2)GPI-specific antibody 26 was compared in C57BL/6 (Th1 prone) and BALB/c (Th2 prone) mice. Results Tetanus toxoid hyper-immunization of BALB/c mice led to reduction in fertility, but in C57BL/6 mice a decrease in fecundity occurred. In both cases, pathology was caused by anti-beta(2)GPI antibodies, the production of which was adjuvant and strain dependent. Conclusion We conclude that TTd immunization and i.v. application of monoclonal antibody 26 induced the same reproductive pathology and that the type of pathology is strain dependent.
PB  - Wiley-Blackwell, Hoboken
T2  - American Journal of Reproductive Immunology
T1  - Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice
EP  - 502
IS  - 5
SP  - 492
VL  - 65
DO  - 10.1111/j.1600-0897.2010.00922.x
UR  - conv_263
ER  - 
@article{
author = "Živković, Irena and Stojanović, Marijana and Petrušić, Vladimir and Inić-Kanada, Aleksandra and Dimitrijević, Ljiljana",
year = "2011",
abstract = "Problem The antiphospholipid syndrome (APS) is a systemic autoimmune disease characterized by vascular thrombosis and/or pregnancy complications (lower fecundity and lower litter size), as well as by an increase in anti-beta(2) glycoprotein I (beta(2)GPI)-specific autoantibody titer. We have investigated how the genetic background of the immune system [T helper (Th) prevalence] and the type of animal model of APS influence the induced pathology. Method of Study Antiphospholipid syndrome induced by tetanus toxoid (TTd) hyper-immunization and by intravenous application of monoclonal anti-beta(2)GPI-specific antibody 26 was compared in C57BL/6 (Th1 prone) and BALB/c (Th2 prone) mice. Results Tetanus toxoid hyper-immunization of BALB/c mice led to reduction in fertility, but in C57BL/6 mice a decrease in fecundity occurred. In both cases, pathology was caused by anti-beta(2)GPI antibodies, the production of which was adjuvant and strain dependent. Conclusion We conclude that TTd immunization and i.v. application of monoclonal antibody 26 induced the same reproductive pathology and that the type of pathology is strain dependent.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "American Journal of Reproductive Immunology",
title = "Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice",
pages = "502-492",
number = "5",
volume = "65",
doi = "10.1111/j.1600-0897.2010.00922.x",
url = "conv_263"
}
Živković, I., Stojanović, M., Petrušić, V., Inić-Kanada, A.,& Dimitrijević, L.. (2011). Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice. in American Journal of Reproductive Immunology
Wiley-Blackwell, Hoboken., 65(5), 492-502.
https://doi.org/10.1111/j.1600-0897.2010.00922.x
conv_263
Živković I, Stojanović M, Petrušić V, Inić-Kanada A, Dimitrijević L. Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice. in American Journal of Reproductive Immunology. 2011;65(5):492-502.
doi:10.1111/j.1600-0897.2010.00922.x
conv_263 .
Živković, Irena, Stojanović, Marijana, Petrušić, Vladimir, Inić-Kanada, Aleksandra, Dimitrijević, Ljiljana, "Induction of APS after TTd Hyper-Immunization has a Different Outcome in BALB/c and C57BL/6 Mice" in American Journal of Reproductive Immunology, 65, no. 5 (2011):492-502,
https://doi.org/10.1111/j.1600-0897.2010.00922.x .,
conv_263 .
21
18

Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population

Burazer, Lidija; Milovanović, K.; Milovanović, Mina; Vučković, Olga; Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2011)

TY  - JOUR
AU  - Burazer, Lidija
AU  - Milovanović, K.
AU  - Milovanović, Mina
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - http://intor.torlakinstitut.com/handle/123456789/320
AB  - House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.
PB  - Wiley, Hoboken
T2  - Medical and Veterinary Entomology
T1  - Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population
EP  - 83
IS  - 1
SP  - 77
VL  - 25
DO  - 10.1111/j.1365-2915.2010.00906.x
UR  - conv_262
ER  - 
@article{
author = "Burazer, Lidija and Milovanović, K. and Milovanović, Mina and Vučković, Olga and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija",
year = "2011",
abstract = "House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.",
publisher = "Wiley, Hoboken",
journal = "Medical and Veterinary Entomology",
title = "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population",
pages = "83-77",
number = "1",
volume = "25",
doi = "10.1111/j.1365-2915.2010.00906.x",
url = "conv_262"
}
Burazer, L., Milovanović, K., Milovanović, M., Vučković, O., Ćirković-Veličković, T.,& Gavrović-Jankulović, M.. (2011). Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology
Wiley, Hoboken., 25(1), 77-83.
https://doi.org/10.1111/j.1365-2915.2010.00906.x
conv_262
Burazer L, Milovanović K, Milovanović M, Vučković O, Ćirković-Veličković T, Gavrović-Jankulović M. Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology. 2011;25(1):77-83.
doi:10.1111/j.1365-2915.2010.00906.x
conv_262 .
Burazer, Lidija, Milovanović, K., Milovanović, Mina, Vučković, Olga, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population" in Medical and Veterinary Entomology, 25, no. 1 (2011):77-83,
https://doi.org/10.1111/j.1365-2915.2010.00906.x .,
conv_262 .
6
6
9

Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein

Stanić, Dragana; Monogioudi, Evanthia; Dilek, Ercili; Radosavljević, Jelena; Atanasković-Marković, Marina; Vučković, Olga; Raija, Lantto; Mattinen, Maija; Buchert, Johanna; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2010)

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/294
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
EP  - 1284
IS  - 9
SP  - 1273
VL  - 54
DO  - 10.1002/mnfr.200900184
UR  - conv_258
ER  - 
@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vučković, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
pages = "1284-1273",
number = "9",
volume = "54",
doi = "10.1002/mnfr.200900184",
url = "conv_258"
}
Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vučković, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley, Hoboken., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184
conv_258
Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vučković O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184
conv_258 .
Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vučković, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 .,
conv_258 .
6
69
66
68

Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization

Živković, Irena; Stojanović, Marijana; Petrušić, Vladimir; Inić-Kanada, Aleksandra; Mićić, Mileva; Dimitrijević, Ljiljana

(Soc Biolgia Chile, Santiago, 2010)

TY  - JOUR
AU  - Živković, Irena
AU  - Stojanović, Marijana
AU  - Petrušić, Vladimir
AU  - Inić-Kanada, Aleksandra
AU  - Mićić, Mileva
AU  - Dimitrijević, Ljiljana
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/306
AB  - We have already demonstrated (Stojanovic et al., 2009) a connection between tetanus toxoid (TTd) hyperimmunization and the induction of anti-phospholipid syndrome (APS) in BALB/c mice. Here we show that C57BL/6 mice subjected to an identical procedure do not exhibit any like pathology attributable to anti-phospholipid antibodies; we explain that this absence results from idiotypic connectivity. Six groups of C57BL/6 mice were hyperimmunized with TTd in aluminum hydroxide or glycerol, with or without pretreatments. Pretreated mice had been injected with polyclonal or nonspecific immune stimulators, such as complete Freund's adjuvant (CFA) or glycerol. The epitope specificity of induced antibodies was tested by indirect ELISA using a tetanus toxoid immunogen and these autoantigens: phospholipids, gangliosides, laminin. Idiotypic connectivity was tested by competitive ELISA and gauged from the degree to which the interaction of idiotypic/anti-idiotypic complementary antibodies was inhibited in the presence of immunized sera antibodies. Higher idiotypic connectivity was noted amongst pretreated mice. There was a positive correlation between higher connectivity and autoantibody levels that acted to favor the participation of natural autoantibodies in the inhibitory process. We conclude that idiotypic connectivity plays a protective role in immunization-induced autoimmunity.
PB  - Soc Biolgia Chile, Santiago
T2  - Biological Research
T1  - Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization
EP  - 402
IS  - 4
SP  - 393
VL  - 43
DO  - 10.4067/S0716-97602010000400003
UR  - conv_261
ER  - 
@article{
author = "Živković, Irena and Stojanović, Marijana and Petrušić, Vladimir and Inić-Kanada, Aleksandra and Mićić, Mileva and Dimitrijević, Ljiljana",
year = "2010",
abstract = "We have already demonstrated (Stojanovic et al., 2009) a connection between tetanus toxoid (TTd) hyperimmunization and the induction of anti-phospholipid syndrome (APS) in BALB/c mice. Here we show that C57BL/6 mice subjected to an identical procedure do not exhibit any like pathology attributable to anti-phospholipid antibodies; we explain that this absence results from idiotypic connectivity. Six groups of C57BL/6 mice were hyperimmunized with TTd in aluminum hydroxide or glycerol, with or without pretreatments. Pretreated mice had been injected with polyclonal or nonspecific immune stimulators, such as complete Freund's adjuvant (CFA) or glycerol. The epitope specificity of induced antibodies was tested by indirect ELISA using a tetanus toxoid immunogen and these autoantigens: phospholipids, gangliosides, laminin. Idiotypic connectivity was tested by competitive ELISA and gauged from the degree to which the interaction of idiotypic/anti-idiotypic complementary antibodies was inhibited in the presence of immunized sera antibodies. Higher idiotypic connectivity was noted amongst pretreated mice. There was a positive correlation between higher connectivity and autoantibody levels that acted to favor the participation of natural autoantibodies in the inhibitory process. We conclude that idiotypic connectivity plays a protective role in immunization-induced autoimmunity.",
publisher = "Soc Biolgia Chile, Santiago",
journal = "Biological Research",
title = "Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization",
pages = "402-393",
number = "4",
volume = "43",
doi = "10.4067/S0716-97602010000400003",
url = "conv_261"
}
Živković, I., Stojanović, M., Petrušić, V., Inić-Kanada, A., Mićić, M.,& Dimitrijević, L.. (2010). Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization. in Biological Research
Soc Biolgia Chile, Santiago., 43(4), 393-402.
https://doi.org/10.4067/S0716-97602010000400003
conv_261
Živković I, Stojanović M, Petrušić V, Inić-Kanada A, Mićić M, Dimitrijević L. Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization. in Biological Research. 2010;43(4):393-402.
doi:10.4067/S0716-97602010000400003
conv_261 .
Živković, Irena, Stojanović, Marijana, Petrušić, Vladimir, Inić-Kanada, Aleksandra, Mićić, Mileva, Dimitrijević, Ljiljana, "Network connectivity is shown to change in C57BL/6 mice during a continuing immune response subsequent to tetanus toxoid hyperimmunization" in Biological Research, 43, no. 4 (2010):393-402,
https://doi.org/10.4067/S0716-97602010000400003 .,
conv_261 .
6
5
6

Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy

Popović, Milica; Milovanović, Mina; Burazer, Lidija; Vučković, Olga; Hoffmann-Sommergruber, Karin; Knulst, Andre C.; Lindner, Buko; Petersen, Arnd; Jankov, Ratko; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2010)

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
UR  - conv_251
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",
url = "conv_251"
}
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
conv_251
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
conv_251 .
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 .,
conv_251 .
12
11
12

Evaluation of the thermal stability and digestibility of heterologously produced banana lectin

Dimitrijević, Rajna; Jadranin, Milka; Burazer, Lidija; Ostojić, Sanja; Gavrović-Jankulović, Marija

(Elsevier Sci Ltd, Oxford, 2010)

TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Jadranin, Milka
AU  - Burazer, Lidija
AU  - Ostojić, Sanja
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/301
AB  - The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT). (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Evaluation of the thermal stability and digestibility of heterologously produced banana lectin
EP  - 1118
IS  - 4
SP  - 1113
VL  - 120
DO  - 10.1016/j.foodchem.2009.11.062
UR  - conv_248
ER  - 
@article{
author = "Dimitrijević, Rajna and Jadranin, Milka and Burazer, Lidija and Ostojić, Sanja and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "The thermal stability of recombinant mannose-specific banana lectin (rBanLec), as well as its stability under conditions of simulated gastro-intestinal fluid (SGF), was investigated. rBanLec was heterologously produced in Escherichia coli, Molecular mass of rBanLec, assessed by ESI-TOF mass spectrometry, was 15972.2 Da. Thermodynamic parameters for rBanLec denaturation, obtained by differential scanning calorimetry (DSC), revealed a transition maximum temperature (T-m) of 60.8 degrees C, calorimetric enthalpy (H-cal) of 136.17 kcal/mol and van't Hoff enthalpy (H-VH) of 50.27 kcal/mol. rBanLec was stable following an incubation for 2 h in SGF, and then for I h, in the simulated intestinal fluid (SIF). Intact primary structure, biological and immunological reactivity of rBanLec were all preserved following treatment under SGF and SIF conditions. In conclusion, rBanLec is a good candidate for the novel bioadhesive lectin-based drug delivery systems to the gastro-intestinal tract (GIT). (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin",
pages = "1118-1113",
number = "4",
volume = "120",
doi = "10.1016/j.foodchem.2009.11.062",
url = "conv_248"
}
Dimitrijević, R., Jadranin, M., Burazer, L., Ostojić, S.,& Gavrović-Jankulović, M.. (2010). Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(4), 1113-1118.
https://doi.org/10.1016/j.foodchem.2009.11.062
conv_248
Dimitrijević R, Jadranin M, Burazer L, Ostojić S, Gavrović-Jankulović M. Evaluation of the thermal stability and digestibility of heterologously produced banana lectin. in Food Chemistry. 2010;120(4):1113-1118.
doi:10.1016/j.foodchem.2009.11.062
conv_248 .
Dimitrijević, Rajna, Jadranin, Milka, Burazer, Lidija, Ostojić, Sanja, Gavrović-Jankulović, Marija, "Evaluation of the thermal stability and digestibility of heterologously produced banana lectin" in Food Chemistry, 120, no. 4 (2010):1113-1118,
https://doi.org/10.1016/j.foodchem.2009.11.062 .,
conv_248 .
14
14
15

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

Stojanović, Marijana; Živković, Irena; Petrušić, Vladimir; Kosec, Duško; Dimitrijević, Rajna; Jankov, Ratko; Dimitrijević, Ljiljana; Gavrović-Jankulović, Marija

(Elsevier, Amsterdam, 2010)

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
UR  - conv_246
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",
url = "conv_246"
}
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
conv_246
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
conv_246 .
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 .,
conv_246 .
18
18
22

Stability evaluation of house dust mite vaccines for sublingual immunotherapy

Burazer, Lidija; Milovanović, Katarina; Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2010)

TY  - JOUR
AU  - Burazer, Lidija
AU  - Milovanović, Katarina
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/314
AB  - Allergen-specific immunotherapy with house dust mite (HDM) allergen extracts can effectively alleviate the symptoms of allergic rhinitis and asthma. The efficacy of the immunotherapeutic treatment is highly dependent on the quality of house dust mite vaccines. This study was performed to assess the stability of house dust mite allergen vaccines prepared for sublingual immunotherapy. Lyophilized Dermatophagoides pteronyssinus (Dpt) mite bodies were the starting material for the production of sublingual vaccines in four therapeutic concentrations. The stability of the extract for vaccine production, which was stored below 4 °C for one month, showed consistence in the protein profile in SDS PAGE. ELISA-inhibition showed that the potencies of Dpt vaccines during a 12 month period were to 65-80 % preserved at all analyzed therapeutic concentrations. This study showed that glycerinated Dpt vaccines stored at 4°C preserved their IgE-binding potential during a 12 month period, implying their suitability for sublingual immunotherapeutic treatment of HDM allergy.
AB  - Alergen-specifična imunoterapija predstavlja postupak koji može da promeni tok bolesti kod alergijskog rinitisa i astme. Kvalitet vakcine pripremljene od kućnih grinja značajno utiče na efikasnost imunoterapeutskog tretmana. Ispitivanje je imalo za cilj procenu stabilnosti vakcine kućnih grinja namenjene za sublingvalnu imunoterapiju. Telo liofilozovanih Dermatophagoides pteronyssinus grinja (Dpt-grinja) upotrebljeno je kao polazni materijal za proizvodnju sublingvalne vakcine u 4 različita terapeutska razblaženja. Potentnost Dpt vakcina praćena ELISA-inhibicijom u 4 terapeutska razblaženja, nakon 12 meseci zadržan je u svim razblaženjima u opsegu 65-80%. Ispitivanje je pokazalo da glicerolom stabilizovane Dpt vakcine za subligvalnu imunoterapiju, uz čuvanje na 4°C zadržavaju alergeni potencijal ( gt 65%) nakon 12 meseci od njihove pripreme, i kao takve mogu se koristiti za tretman alergije na kućne grinje.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Stability evaluation of house dust mite vaccines for sublingual immunotherapy
T1  - Ispitivanje stabilnosti vakcine kućne prašine za sublingvalnu imunoterapiju
EP  - 26
IS  - 1
SP  - 19
VL  - 75
DO  - 10.2298/JSC1001019B
UR  - conv_23
ER  - 
@article{
author = "Burazer, Lidija and Milovanović, Katarina and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Allergen-specific immunotherapy with house dust mite (HDM) allergen extracts can effectively alleviate the symptoms of allergic rhinitis and asthma. The efficacy of the immunotherapeutic treatment is highly dependent on the quality of house dust mite vaccines. This study was performed to assess the stability of house dust mite allergen vaccines prepared for sublingual immunotherapy. Lyophilized Dermatophagoides pteronyssinus (Dpt) mite bodies were the starting material for the production of sublingual vaccines in four therapeutic concentrations. The stability of the extract for vaccine production, which was stored below 4 °C for one month, showed consistence in the protein profile in SDS PAGE. ELISA-inhibition showed that the potencies of Dpt vaccines during a 12 month period were to 65-80 % preserved at all analyzed therapeutic concentrations. This study showed that glycerinated Dpt vaccines stored at 4°C preserved their IgE-binding potential during a 12 month period, implying their suitability for sublingual immunotherapeutic treatment of HDM allergy., Alergen-specifična imunoterapija predstavlja postupak koji može da promeni tok bolesti kod alergijskog rinitisa i astme. Kvalitet vakcine pripremljene od kućnih grinja značajno utiče na efikasnost imunoterapeutskog tretmana. Ispitivanje je imalo za cilj procenu stabilnosti vakcine kućnih grinja namenjene za sublingvalnu imunoterapiju. Telo liofilozovanih Dermatophagoides pteronyssinus grinja (Dpt-grinja) upotrebljeno je kao polazni materijal za proizvodnju sublingvalne vakcine u 4 različita terapeutska razblaženja. Potentnost Dpt vakcina praćena ELISA-inhibicijom u 4 terapeutska razblaženja, nakon 12 meseci zadržan je u svim razblaženjima u opsegu 65-80%. Ispitivanje je pokazalo da glicerolom stabilizovane Dpt vakcine za subligvalnu imunoterapiju, uz čuvanje na 4°C zadržavaju alergeni potencijal ( gt 65%) nakon 12 meseci od njihove pripreme, i kao takve mogu se koristiti za tretman alergije na kućne grinje.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Stability evaluation of house dust mite vaccines for sublingual immunotherapy, Ispitivanje stabilnosti vakcine kućne prašine za sublingvalnu imunoterapiju",
pages = "26-19",
number = "1",
volume = "75",
doi = "10.2298/JSC1001019B",
url = "conv_23"
}
Burazer, L., Milovanović, K., Ćirković-Veličković, T.,& Gavrović-Jankulović, M.. (2010). Stability evaluation of house dust mite vaccines for sublingual immunotherapy. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 75(1), 19-26.
https://doi.org/10.2298/JSC1001019B
conv_23
Burazer L, Milovanović K, Ćirković-Veličković T, Gavrović-Jankulović M. Stability evaluation of house dust mite vaccines for sublingual immunotherapy. in Journal of the Serbian Chemical Society. 2010;75(1):19-26.
doi:10.2298/JSC1001019B
conv_23 .
Burazer, Lidija, Milovanović, Katarina, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, "Stability evaluation of house dust mite vaccines for sublingual immunotherapy" in Journal of the Serbian Chemical Society, 75, no. 1 (2010):19-26,
https://doi.org/10.2298/JSC1001019B .,
conv_23 .

Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment

Petrušić, Vladimir; Stojanović, Marijana; Živković, Irena; Inić-Kanada, Aleksandra; Dimitrijević, Ljiljana

(Taylor & Francis Inc, Philadelphia, 2010)

TY  - JOUR
AU  - Petrušić, Vladimir
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Inić-Kanada, Aleksandra
AU  - Dimitrijević, Ljiljana
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/295
AB  - IgM is the first antibody produced during the immune response to infection or immunization, and it can be secreted as pentamer (containing a small polypeptide, termed as J chain) or hexamer (lacking J chain). In this paper we have analyzed structural characteristics (by electrophoresis and immunoblot) and anti-bacterial specificity (by enzyme-linked immunosorbent assay) of IgM antibodies purified from female patients suffering from recurrent bacterial infections of lower urinary tract and therapeutically immunized with the mixture of heat-inactivated uropathogenic bacteria. We report on changes in the composition of IgM polymers in tested patients. The immunization induced the raise of the levels of hexamers in patients that did not respond to immunization (non-responders), while the IgM polymers remained on the pentameric level in immunization dependent responders. We propose that the composition of IgM polymers could influence the immunization outcome and should be taken in count regarding the treatment of recurrent bacterial infections.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Immunological Investigations
T1  - Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment
EP  - 795
IS  - 8
SP  - 781
VL  - 39
DO  - 10.3109/08820139.2010.497831
UR  - conv_259
ER  - 
@article{
author = "Petrušić, Vladimir and Stojanović, Marijana and Živković, Irena and Inić-Kanada, Aleksandra and Dimitrijević, Ljiljana",
year = "2010",
abstract = "IgM is the first antibody produced during the immune response to infection or immunization, and it can be secreted as pentamer (containing a small polypeptide, termed as J chain) or hexamer (lacking J chain). In this paper we have analyzed structural characteristics (by electrophoresis and immunoblot) and anti-bacterial specificity (by enzyme-linked immunosorbent assay) of IgM antibodies purified from female patients suffering from recurrent bacterial infections of lower urinary tract and therapeutically immunized with the mixture of heat-inactivated uropathogenic bacteria. We report on changes in the composition of IgM polymers in tested patients. The immunization induced the raise of the levels of hexamers in patients that did not respond to immunization (non-responders), while the IgM polymers remained on the pentameric level in immunization dependent responders. We propose that the composition of IgM polymers could influence the immunization outcome and should be taken in count regarding the treatment of recurrent bacterial infections.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Immunological Investigations",
title = "Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment",
pages = "795-781",
number = "8",
volume = "39",
doi = "10.3109/08820139.2010.497831",
url = "conv_259"
}
Petrušić, V., Stojanović, M., Živković, I., Inić-Kanada, A.,& Dimitrijević, L.. (2010). Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment. in Immunological Investigations
Taylor & Francis Inc, Philadelphia., 39(8), 781-795.
https://doi.org/10.3109/08820139.2010.497831
conv_259
Petrušić V, Stojanović M, Živković I, Inić-Kanada A, Dimitrijević L. Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment. in Immunological Investigations. 2010;39(8):781-795.
doi:10.3109/08820139.2010.497831
conv_259 .
Petrušić, Vladimir, Stojanović, Marijana, Živković, Irena, Inić-Kanada, Aleksandra, Dimitrijević, Ljiljana, "Changes in Composition of IgM Polymers in Patients Suffering from Recurrent Urinary Bacterial Infections after Bacterial Immunization Treatment" in Immunological Investigations, 39, no. 8 (2010):781-795,
https://doi.org/10.3109/08820139.2010.497831 .,
conv_259 .
6
5
6

Removal of N-terminal peptides from β-lactoglobulin by proteolytic contaminants in a commercial phenol oxidase preparation

Stanić, Dragana; Radosavljević, Jelena; Polović, Natalija; Jadranin, Milka; Popović, Milica; Vučković, Olga; Burazer, Lidija; Jankov, Ratko; Veličković, Tanja

(2009)

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
UR  - conv_543
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",
url = "conv_543"
}
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
conv_543
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
conv_543 .
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 .,
conv_543 .
6
8
8

Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus

Milovanović, Katarina; Burazer, Lidija; Vučković, Olga; Atanasković-Marković, Marina; Ćirković-Veličković, Tanja; Jankov, Ratko; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2009)

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
UR  - conv_22
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",
url = "conv_22"
}
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
conv_22
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
conv_22 .
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 .,
conv_22 .
1
1

Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation

Perović, I.; Milovanović, Mina; Stanić, Dragana; Burazer, Lidija; Petrović, D.; Milčić-Matić, Natalija; Gafvelink, G.; van Hage, Marianne; Jankov, Ratko; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2009)

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
UR  - conv_227
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",
url = "conv_227"
}
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
conv_227
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
conv_227 .
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 .,
conv_227 .
9
9
9

The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68

Dimitrijević, Rajna; Stojanović, Marijana; Živković, Irena; Petersen, Arnd; Jankov, Ratko; Dimitrijević, Ljiljana; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2009)

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
UR  - conv_244
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",
url = "conv_244"
}
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
conv_244
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
conv_244 .
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 .,
conv_244 .
6
26
21
25

The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications

Inić-Kanada, Aleksandra; Stojanović, Marijana; Živković, Irena; Petrušić, Vladimir; Dimitrijević, Ljiljana

(Srpsko hemijsko društvo, Beograd, 2009)

TY  - JOUR
AU  - Inić-Kanada, Aleksandra
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Petrušić, Vladimir
AU  - Dimitrijević, Ljiljana
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/287
AB  - A murine monoclonal IgG1 antibody, marked as MAb26, specific for tetanus toxoid has been immunochemically characterized. By performing enzyme-linked immunosorbent assays (ELISAs) and western blot analyses, it was demonstrated that MAb26 reacted with tetanus toxoid, tetanus toxin and β2-glycoprotein I (β2GPI). According to the results, MAb26 recognized the sequential epitope on the tetanus heavy chain. The affinity constant, calculated from Scatchard plots of MAb26 binding to tetanus toxoid, was 1.145×108 M-1 and the measurement of the relative affinity of MAb26 by ELISA using thiocyanate elution showed a significantly higher affinity of MAb26 to the toxoid (p = 0.0012) in comparison to the toxin. Additionally, the reactivity of MAb26 toward the toxoid forms increased when the tetanus toxin was detoxified using 8 mM and higher formaldehyde concentrations. The similarity of the tetanus toxoid to several sera proteins, either at the level of its conformation (IL-1α) or at the level of peptide sequences (â2GPI, laminin) favors its role in autoimmunity by the mechanism of molecular mimicry. As the induction of an autoimmune disease is dependent on the breakdown of tolerance, which could be the result of an overt hyperstimulation, the control of the presence and concentration of self-reactive epitopes in vaccine preparations is a prerequisite. In this study, it was shown that MAb26 can: 1) discriminate between the tetanus toxin and different toxoid forms, which makes it a good candidate for antibody control during vaccine preparation; 2) due to its cross-reactivity with β2GPI, it could provide information on the presence of a potentially dangerous sequential epitope expressed at the protein surface.
AB  - Ovaj rad opisuje imunohemijsku karakterizaciju mišjeg IgG1 monoklonskog antitela označenog kao MAt26. Enzimskim imunosorbentnim testom (ELISA) i Western blot analizom je pokazano da MAt26 reaguje sa tetanus toksoidom, tetanus toksinom i β2-glikoproteinom I (β2GPI). Prema našim rezultatima, MAt26 prepoznaje sekvencioni epitop na teškom lancu molekula tetanusa. Konstanta afiniteta MAt26 za tetanus toksoid, izračunata na osnovu Skačardovog dijagrama, je 1,145×108 M-1. Na osnovu elucije tiocijanatom, korišćene za određivanje relativnog afiniteta MAt26 za tetanus toksin i tetanus toksoid, postupkom baziranim na ELISA-i, pokazan je znatno veći (p = 0,0012) afinitet MAt26 ka toksoidnoj formi. Takođe, reaktivnost MAt26 ka toksoidnoj formi rasla je sa porastom koncentracije formaldehida, počevši od 8 mM, korišćenog u procesu detoksifikacije. Sličnost tetanus toksoida sa različitim serumskim proteinima na nivou konformacije i/ili peptidnih sekvencija (β2GPI, laminin) ukazuje na njegovu potencijalnu ulogu u indukciji autoimunosti mehanizmom molekulske mimikrije. Budući da nastanak autoimunske bolesti podrazumeva narušavanje tolerancije, na primer, prekomernom stimulacijom imunskog sistema, kontrola prisustva i koncentracije sebi sličnih epitopa se nameće kao neophodna. U ovom radu je pokazano da: 1) MAt26 može da pravi razliku između tetanus toksina i različitih toksoidnih formi što ga čini potencijalno dobrim antitelom koje bi se koristilo u kontroli tokom proizvodnje vakcina; 2) zahvaljujući unakrsnoj reaktivnosti sa β2GPI, MAt26 može da pruži informacije o prisustvu potencijalno opasnih epitopa na površini proteina.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications
T1  - Monoklonsko antitelo 26 napravljeno na tetanus toksoidu reaguje i sa tetanus toksinom i β2-glikoproteinom I - karakteristike vezivanja in vitro i moguća primena
EP  - 257
IS  - 3
SP  - 245
VL  - 74
DO  - 10.2298/JSC0903245I
UR  - conv_20
ER  - 
@article{
author = "Inić-Kanada, Aleksandra and Stojanović, Marijana and Živković, Irena and Petrušić, Vladimir and Dimitrijević, Ljiljana",
year = "2009",
abstract = "A murine monoclonal IgG1 antibody, marked as MAb26, specific for tetanus toxoid has been immunochemically characterized. By performing enzyme-linked immunosorbent assays (ELISAs) and western blot analyses, it was demonstrated that MAb26 reacted with tetanus toxoid, tetanus toxin and β2-glycoprotein I (β2GPI). According to the results, MAb26 recognized the sequential epitope on the tetanus heavy chain. The affinity constant, calculated from Scatchard plots of MAb26 binding to tetanus toxoid, was 1.145×108 M-1 and the measurement of the relative affinity of MAb26 by ELISA using thiocyanate elution showed a significantly higher affinity of MAb26 to the toxoid (p = 0.0012) in comparison to the toxin. Additionally, the reactivity of MAb26 toward the toxoid forms increased when the tetanus toxin was detoxified using 8 mM and higher formaldehyde concentrations. The similarity of the tetanus toxoid to several sera proteins, either at the level of its conformation (IL-1α) or at the level of peptide sequences (â2GPI, laminin) favors its role in autoimmunity by the mechanism of molecular mimicry. As the induction of an autoimmune disease is dependent on the breakdown of tolerance, which could be the result of an overt hyperstimulation, the control of the presence and concentration of self-reactive epitopes in vaccine preparations is a prerequisite. In this study, it was shown that MAb26 can: 1) discriminate between the tetanus toxin and different toxoid forms, which makes it a good candidate for antibody control during vaccine preparation; 2) due to its cross-reactivity with β2GPI, it could provide information on the presence of a potentially dangerous sequential epitope expressed at the protein surface., Ovaj rad opisuje imunohemijsku karakterizaciju mišjeg IgG1 monoklonskog antitela označenog kao MAt26. Enzimskim imunosorbentnim testom (ELISA) i Western blot analizom je pokazano da MAt26 reaguje sa tetanus toksoidom, tetanus toksinom i β2-glikoproteinom I (β2GPI). Prema našim rezultatima, MAt26 prepoznaje sekvencioni epitop na teškom lancu molekula tetanusa. Konstanta afiniteta MAt26 za tetanus toksoid, izračunata na osnovu Skačardovog dijagrama, je 1,145×108 M-1. Na osnovu elucije tiocijanatom, korišćene za određivanje relativnog afiniteta MAt26 za tetanus toksin i tetanus toksoid, postupkom baziranim na ELISA-i, pokazan je znatno veći (p = 0,0012) afinitet MAt26 ka toksoidnoj formi. Takođe, reaktivnost MAt26 ka toksoidnoj formi rasla je sa porastom koncentracije formaldehida, počevši od 8 mM, korišćenog u procesu detoksifikacije. Sličnost tetanus toksoida sa različitim serumskim proteinima na nivou konformacije i/ili peptidnih sekvencija (β2GPI, laminin) ukazuje na njegovu potencijalnu ulogu u indukciji autoimunosti mehanizmom molekulske mimikrije. Budući da nastanak autoimunske bolesti podrazumeva narušavanje tolerancije, na primer, prekomernom stimulacijom imunskog sistema, kontrola prisustva i koncentracije sebi sličnih epitopa se nameće kao neophodna. U ovom radu je pokazano da: 1) MAt26 može da pravi razliku između tetanus toksina i različitih toksoidnih formi što ga čini potencijalno dobrim antitelom koje bi se koristilo u kontroli tokom proizvodnje vakcina; 2) zahvaljujući unakrsnoj reaktivnosti sa β2GPI, MAt26 može da pruži informacije o prisustvu potencijalno opasnih epitopa na površini proteina.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications, Monoklonsko antitelo 26 napravljeno na tetanus toksoidu reaguje i sa tetanus toksinom i β2-glikoproteinom I - karakteristike vezivanja in vitro i moguća primena",
pages = "257-245",
number = "3",
volume = "74",
doi = "10.2298/JSC0903245I",
url = "conv_20"
}
Inić-Kanada, A., Stojanović, M., Živković, I., Petrušić, V.,& Dimitrijević, L.. (2009). The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 74(3), 245-257.
https://doi.org/10.2298/JSC0903245I
conv_20
Inić-Kanada A, Stojanović M, Živković I, Petrušić V, Dimitrijević L. The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications. in Journal of the Serbian Chemical Society. 2009;74(3):245-257.
doi:10.2298/JSC0903245I
conv_20 .
Inić-Kanada, Aleksandra, Stojanović, Marijana, Živković, Irena, Petrušić, Vladimir, Dimitrijević, Ljiljana, "The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications" in Journal of the Serbian Chemical Society, 74, no. 3 (2009):245-257,
https://doi.org/10.2298/JSC0903245I .,
conv_20 .
4
4
4

Chemical modification of Art v 1, a major mugwort pollen allergen, by cis-aconitylation and citraconylation

Stanić, Dragana; Burazer, Lidija; Gavrović-Jankulović, Marija; Jankov, Ratko; Ćirković-Veličković, Tanja

(Srpsko hemijsko društvo, Beograd, 2009)

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
UR  - conv_21
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",
url = "conv_21"
}
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
conv_21
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
conv_21 .
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 .,
conv_21 .
3
3
4

The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response

Stojanović, Marijana; Živković, Irena; Inić-Kanada, Aleksandra; Petrušić, Vladimir; Mićić, Mileva; Dimitrijević, Ljiljana

(Wiley, Hoboken, 2009)

TY  - JOUR
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Inić-Kanada, Aleksandra
AU  - Petrušić, Vladimir
AU  - Mićić, Mileva
AU  - Dimitrijević, Ljiljana
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/284
AB  - Results are presented concerning our attempts to create a suitable model system for studying the connection between microbial antigen (micAg), autoimmunity and autoimmune disease on the basis of hyper-immunization and application of micAg in different contexts. Our research was focused on tetanus toxoid (TTd) as a model micAg. Non-pretreated and complete Freund's adjuvant pretreated BALB/c mice were immunized with high doses of TTd mixed with glycerol or aluminum hydroxide as adjuvants. The main aims of the experiments were to evaluate the properties of induced humoral immune responses, evaluate the pathological potential of induced immune responses and determine possible correlations between the properties of a humoral immune response and its pathological potential. The production of TTd-specific and self-reactive beta(2)-glycoprotein I (beta(2)-GP I)-specific antibodies (Abs) was detected in all groups but with specific, context-related properties. Analysis of pregnancy-related pathology (anti-beta(2)-GP I Abs-associated) showed differences in the pathological potential of the induced immune response. It was demonstrated that severity of pathology is positively correlated to the abundance of IgG that recognizes beta(2)-GP I adsorbed onto phosphatidylserine, and to IgG affinity. Furthermore, it was demonstrated that molecular mimicry, which results in generation of anti-beta(2)-GP I Abs upon TTd immunization, is necessary but not sufficient for the development of pregnancy-related pathology.
PB  - Wiley, Hoboken
T2  - Microbiology and Immunology
T1  - The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response
EP  - 100
IS  - 2
SP  - 89
VL  - 53
DO  - 10.1111/j.1348-0421.2008.00094.x
UR  - conv_230
ER  - 
@article{
author = "Stojanović, Marijana and Živković, Irena and Inić-Kanada, Aleksandra and Petrušić, Vladimir and Mićić, Mileva and Dimitrijević, Ljiljana",
year = "2009",
abstract = "Results are presented concerning our attempts to create a suitable model system for studying the connection between microbial antigen (micAg), autoimmunity and autoimmune disease on the basis of hyper-immunization and application of micAg in different contexts. Our research was focused on tetanus toxoid (TTd) as a model micAg. Non-pretreated and complete Freund's adjuvant pretreated BALB/c mice were immunized with high doses of TTd mixed with glycerol or aluminum hydroxide as adjuvants. The main aims of the experiments were to evaluate the properties of induced humoral immune responses, evaluate the pathological potential of induced immune responses and determine possible correlations between the properties of a humoral immune response and its pathological potential. The production of TTd-specific and self-reactive beta(2)-glycoprotein I (beta(2)-GP I)-specific antibodies (Abs) was detected in all groups but with specific, context-related properties. Analysis of pregnancy-related pathology (anti-beta(2)-GP I Abs-associated) showed differences in the pathological potential of the induced immune response. It was demonstrated that severity of pathology is positively correlated to the abundance of IgG that recognizes beta(2)-GP I adsorbed onto phosphatidylserine, and to IgG affinity. Furthermore, it was demonstrated that molecular mimicry, which results in generation of anti-beta(2)-GP I Abs upon TTd immunization, is necessary but not sufficient for the development of pregnancy-related pathology.",
publisher = "Wiley, Hoboken",
journal = "Microbiology and Immunology",
title = "The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response",
pages = "100-89",
number = "2",
volume = "53",
doi = "10.1111/j.1348-0421.2008.00094.x",
url = "conv_230"
}
Stojanović, M., Živković, I., Inić-Kanada, A., Petrušić, V., Mićić, M.,& Dimitrijević, L.. (2009). The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response. in Microbiology and Immunology
Wiley, Hoboken., 53(2), 89-100.
https://doi.org/10.1111/j.1348-0421.2008.00094.x
conv_230
Stojanović M, Živković I, Inić-Kanada A, Petrušić V, Mićić M, Dimitrijević L. The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response. in Microbiology and Immunology. 2009;53(2):89-100.
doi:10.1111/j.1348-0421.2008.00094.x
conv_230 .
Stojanović, Marijana, Živković, Irena, Inić-Kanada, Aleksandra, Petrušić, Vladimir, Mićić, Mileva, Dimitrijević, Ljiljana, "The context of tetanus toxoid application influences the outcome of antigen-specific and self-directed humoral immune response" in Microbiology and Immunology, 53, no. 2 (2009):89-100,
https://doi.org/10.1111/j.1348-0421.2008.00094.x .,
conv_230 .
1
11
10
11

Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry

Inić-Kanada, Aleksandra; Stojanović, Marijana; Živković, Irena; Kosec, Duško; Mićić, Mileva; Petrušić, Vladimir; Živančević-Simonović, Snežana; Dimitrijević, Ljiljana

(Wiley, Hoboken, 2009)

TY  - JOUR
AU  - Inić-Kanada, Aleksandra
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Kosec, Duško
AU  - Mićić, Mileva
AU  - Petrušić, Vladimir
AU  - Živančević-Simonović, Snežana
AU  - Dimitrijević, Ljiljana
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/283
AB  - Studies on experimental antiphospholipid syndrome (APS) models proved that molecular mimicry between plasma protein beta(2)-glycoprotein I (beta(2)GPI) and structure within micro-organisms or their products, might be a cause for experimental APS. Considering the heterogeneity of polyclonal antiphospholipid antibodies (aPLs), it is important to define the precise characteristics of pathogenic aPLs. To avoid the influence of polyclonality and to further analyse the connection between molecular mimicry and APS, we produced monoclonal antibodies (MAbs) against tetanus toxoid (TTd) and tested their reactivity against beta(2)GPI. In this report, we analysed the characteristics of MAb26 raised against TTd and cross-reactive with beta(2)GPI: its binding properties in various in vitro immunoassays, its specific interactions with surface epitopes expressed on apoptotic cells and its role in vivo. We have demonstrated that MAb26: (i) binds beta(2)GPI being immobilized on an appropriate surface: irradiated polystyrene plates, non-irradiated plates pre-coated with anionic phospholipids and polyvinylidene fluoride membrane; (ii) binds specifically to apoptotic but not to viable cells and the binding is beta(2)GPI-dependent; and (iii) induces a pathologic pregnancy outcome when passively injected into BALB/c mice. This study concluded that certain subpopulations of antibodies raised against TTd and cross-reactive with beta(2)GPI, because of the molecular mimicry mechanism, could have pathologic potential.
PB  - Wiley, Hoboken
T2  - American Journal of Reproductive Immunology
T1  - Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry
EP  - 51
IS  - 1
SP  - 39
VL  - 61
DO  - 10.1111/j.1600-0897.2008.00660.x
UR  - conv_223
ER  - 
@article{
author = "Inić-Kanada, Aleksandra and Stojanović, Marijana and Živković, Irena and Kosec, Duško and Mićić, Mileva and Petrušić, Vladimir and Živančević-Simonović, Snežana and Dimitrijević, Ljiljana",
year = "2009",
abstract = "Studies on experimental antiphospholipid syndrome (APS) models proved that molecular mimicry between plasma protein beta(2)-glycoprotein I (beta(2)GPI) and structure within micro-organisms or their products, might be a cause for experimental APS. Considering the heterogeneity of polyclonal antiphospholipid antibodies (aPLs), it is important to define the precise characteristics of pathogenic aPLs. To avoid the influence of polyclonality and to further analyse the connection between molecular mimicry and APS, we produced monoclonal antibodies (MAbs) against tetanus toxoid (TTd) and tested their reactivity against beta(2)GPI. In this report, we analysed the characteristics of MAb26 raised against TTd and cross-reactive with beta(2)GPI: its binding properties in various in vitro immunoassays, its specific interactions with surface epitopes expressed on apoptotic cells and its role in vivo. We have demonstrated that MAb26: (i) binds beta(2)GPI being immobilized on an appropriate surface: irradiated polystyrene plates, non-irradiated plates pre-coated with anionic phospholipids and polyvinylidene fluoride membrane; (ii) binds specifically to apoptotic but not to viable cells and the binding is beta(2)GPI-dependent; and (iii) induces a pathologic pregnancy outcome when passively injected into BALB/c mice. This study concluded that certain subpopulations of antibodies raised against TTd and cross-reactive with beta(2)GPI, because of the molecular mimicry mechanism, could have pathologic potential.",
publisher = "Wiley, Hoboken",
journal = "American Journal of Reproductive Immunology",
title = "Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry",
pages = "51-39",
number = "1",
volume = "61",
doi = "10.1111/j.1600-0897.2008.00660.x",
url = "conv_223"
}
Inić-Kanada, A., Stojanović, M., Živković, I., Kosec, D., Mićić, M., Petrušić, V., Živančević-Simonović, S.,& Dimitrijević, L.. (2009). Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry. in American Journal of Reproductive Immunology
Wiley, Hoboken., 61(1), 39-51.
https://doi.org/10.1111/j.1600-0897.2008.00660.x
conv_223
Inić-Kanada A, Stojanović M, Živković I, Kosec D, Mićić M, Petrušić V, Živančević-Simonović S, Dimitrijević L. Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry. in American Journal of Reproductive Immunology. 2009;61(1):39-51.
doi:10.1111/j.1600-0897.2008.00660.x
conv_223 .
Inić-Kanada, Aleksandra, Stojanović, Marijana, Živković, Irena, Kosec, Duško, Mićić, Mileva, Petrušić, Vladimir, Živančević-Simonović, Snežana, Dimitrijević, Ljiljana, "Murine Monoclonal Antibody 26 Raised Against Tetanus Toxoid Cross-Reacts with beta(2)-Glycoprotein I: Its Characteristics and Role in Molecular Mimicry" in American Journal of Reproductive Immunology, 61, no. 1 (2009):39-51,
https://doi.org/10.1111/j.1600-0897.2008.00660.x .,
conv_223 .
22
18
21

Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion

Polović, Natalija; Pjanović, Rada V.; Burazer, Lidija; Velicković, Sava J.; Jankov, Ratko; Ćirković-Veličković, Tanja

(John Wiley & Sons Ltd, Chichester, 2009)

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
UR  - conv_224
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",
url = "conv_224"
}
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
conv_224
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
conv_224 .
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 .,
conv_224 .
17
14
17

Quantification of the thaumatin-like kiwi allergen by a monoclonal antibody-based ELISA

Gavrović-Jankulović, Marija; Spasic, Milena; Veličković, Tanja; Stojanović, Marijana; Inić-Kanada, Aleksandra; Dimitrijevic, Ljiliana; Lindner, Buko; Petersen, Arnd; Becker, Wolf-Meinhard; Jankov, Ratko

(2008)

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
UR  - conv_517
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",
url = "conv_517"
}
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
conv_517
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
conv_517 .
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 .,
conv_517 .
20
16
22

A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro

Polović, Natalija; Blanuša, Milan; Gavrović-Jankulović, Marija; Atanasković-Marković, Marina; Burazer, Lidija; Jankov, Ratko; Veličković, Tanja

(2007)

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
UR  - conv_508
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",
url = "conv_508"
}
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
conv_508
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
conv_508 .
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 .,
conv_508 .
58
45
54

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

Blanuša, Milan; Perović, Iva; Popović, Milica; Polović, Natalija; Burazer, Lidija; Milovanović, Mina; Gavrović-Jankulović, Marija; Jankov, Ratko; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2007)

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
UR  - conv_200
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",
url = "conv_200"
}
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
conv_200
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
conv_200 .
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 .,
conv_200 .
9
7
9