Kukavica, Biljana

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  • Kukavica, Biljana (1)
  • Kukavica, Biljana M (1)
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Author's Bibliography

Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro

Davidović-Plavšić, Biljana; Lukić, Nataša; Nikolić-Kokić, Aleksandra; Kukavica, Biljana

(2019)

TY  - JOUR
AU  - Davidović-Plavšić, Biljana
AU  - Lukić, Nataša
AU  - Nikolić-Kokić, Aleksandra
AU  - Kukavica, Biljana
PY  - 2019
UR  - http://www.doiserbia.nb.rs/Article.aspx?ID=0352-51391800115D
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/3396
AB  - The aim of this work was to investigate the effect of the commercial formulation hemazin SC 500, an herbicide containing terbuthylazine as the active compound, on the isoenzyme patterns and activities of Cu-Zn superoxide dismutase (SOD1) and catalase (CAT), as well as on the glutathione S-transferase (GST) activity, in human erythrocytes in vitro. The human erythrocytes were treated with hemazin SC 500 over a broad range of terbuthylazine concentrations (37 nmol L-1– –37 mol L-1) for 1 and 3 h at a temperature of 37°C. Native electrophoresis of the control and treated samples revealed two SOD1 and one CAT isoform. Treatment did not affect the SOD1 and CAT isoenzyme profile, but induced a change in their activities. Terbuthylazine at lower concentration induced a significant increase of the total SOD1 activity and decreased the GST activity in samples incubated for 1 and 3 h. On the other hand, the highest increase in the CAT activity was observed for the sample treated for 1 h with a higher concentration of terbuthylazine. Hemazin SC 500 containing terbuthylazine induces changes in the erythrocyte antioxidative system whereby the response of individual enzymatic antioxidants depends on the concentration of the pesticide and the incubation time.
T2  - Journal of the Serbian Chemical Society
T1  - Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro
IS  - 5
VL  - 84
DO  - 10.2298/JSC181011115D
SP  - 455
EP  - 465
ER  - 
@article{
author = "Davidović-Plavšić, Biljana and Lukić, Nataša and Nikolić-Kokić, Aleksandra and Kukavica, Biljana",
year = "2019",
abstract = "The aim of this work was to investigate the effect of the commercial formulation hemazin SC 500, an herbicide containing terbuthylazine as the active compound, on the isoenzyme patterns and activities of Cu-Zn superoxide dismutase (SOD1) and catalase (CAT), as well as on the glutathione S-transferase (GST) activity, in human erythrocytes in vitro. The human erythrocytes were treated with hemazin SC 500 over a broad range of terbuthylazine concentrations (37 nmol L-1– –37 mol L-1) for 1 and 3 h at a temperature of 37°C. Native electrophoresis of the control and treated samples revealed two SOD1 and one CAT isoform. Treatment did not affect the SOD1 and CAT isoenzyme profile, but induced a change in their activities. Terbuthylazine at lower concentration induced a significant increase of the total SOD1 activity and decreased the GST activity in samples incubated for 1 and 3 h. On the other hand, the highest increase in the CAT activity was observed for the sample treated for 1 h with a higher concentration of terbuthylazine. Hemazin SC 500 containing terbuthylazine induces changes in the erythrocyte antioxidative system whereby the response of individual enzymatic antioxidants depends on the concentration of the pesticide and the incubation time.",
journal = "Journal of the Serbian Chemical Society",
title = "Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro",
number = "5",
volume = "84",
doi = "10.2298/JSC181011115D",
pages = "455-465"
}
Davidović-Plavšić, B., Lukić, N., Nikolić-Kokić, A.,& Kukavica, B.. (2019). Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro. in Journal of the Serbian Chemical Society, 84(5), 455-465.
https://doi.org/10.2298/JSC181011115D
Davidović-Plavšić B, Lukić N, Nikolić-Kokić A, Kukavica B. Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro. in Journal of the Serbian Chemical Society. 2019;84(5):455-465.
doi:10.2298/JSC181011115D .
Davidović-Plavšić, Biljana, Lukić, Nataša, Nikolić-Kokić, Aleksandra, Kukavica, Biljana, "Effects of hemazin SC 500 (terbuthylazine) on antioxidative enzymes in human erythrocytes in vitro" in Journal of the Serbian Chemical Society, 84, no. 5 (2019):455-465,
https://doi.org/10.2298/JSC181011115D . .
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Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum

Simonić, Jasmina; Stajić, Mirjana M; Kukavica, Biljana M; Vukojević, Jelena B.; Veljović-Jovanović, Sonja D; Duletić-Laušević, Sonja N.

(2010)

TY  - JOUR
AU  - Simonić, Jasmina
AU  - Stajić, Mirjana M
AU  - Kukavica, Biljana M
AU  - Vukojević, Jelena B.
AU  - Veljović-Jovanović, Sonja D
AU  - Duletić-Laušević, Sonja N.
PY  - 2010
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1407
AB  - The purpose of this study was to resolve the question of whether various nitrogen sources and concentrations affect characteristics of selected G. lucidum ligninolytic enzymes participating in wheat straw fermentation. This is the first study reporting the presence of versatile peroxidase activity in crude extract of G. lucidum culture, as well as isoforms profile of Mn-oxidizing peroxidases. NH(4)NO(3) was the optimum nitrogen source for laccase and Mn-dependent peroxidase activity, while peptone was the optimum one for versatile peroxidase activity. Four bands with laccase activity were obtained by native PAGE and IEF separations from medium enriched with inorganic nitrogen source, and only two bands from medium containing organic source. Medium composition was not shown to affect isoenzyme patterns of Mn-oxidizing peroxidases. Four isoforms of Mn-dependent peroxidase and three of versatile peroxidase were obtained on native PAGE. By IEF separation, five isoforms of Mn-dependent peroxidase and only two of versatile peroxidase were observed. The results demonstrated that G. lucidum has potential for mineralization and transformation of various agricultural residues and should take more significant participation in large-scale biotechnological processes.
T2  - Bioresources
T1  - Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum
IS  - 4
VL  - 5
EP  - 2373
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1407
ER  - 
@article{
author = "Simonić, Jasmina and Stajić, Mirjana M and Kukavica, Biljana M and Vukojević, Jelena B. and Veljović-Jovanović, Sonja D and Duletić-Laušević, Sonja N.",
year = "2010",
abstract = "The purpose of this study was to resolve the question of whether various nitrogen sources and concentrations affect characteristics of selected G. lucidum ligninolytic enzymes participating in wheat straw fermentation. This is the first study reporting the presence of versatile peroxidase activity in crude extract of G. lucidum culture, as well as isoforms profile of Mn-oxidizing peroxidases. NH(4)NO(3) was the optimum nitrogen source for laccase and Mn-dependent peroxidase activity, while peptone was the optimum one for versatile peroxidase activity. Four bands with laccase activity were obtained by native PAGE and IEF separations from medium enriched with inorganic nitrogen source, and only two bands from medium containing organic source. Medium composition was not shown to affect isoenzyme patterns of Mn-oxidizing peroxidases. Four isoforms of Mn-dependent peroxidase and three of versatile peroxidase were obtained on native PAGE. By IEF separation, five isoforms of Mn-dependent peroxidase and only two of versatile peroxidase were observed. The results demonstrated that G. lucidum has potential for mineralization and transformation of various agricultural residues and should take more significant participation in large-scale biotechnological processes.",
journal = "Bioresources",
title = "Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum",
number = "4",
volume = "5",
pages = "2373",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1407"
}
Simonić, J., Stajić, M. M., Kukavica, B. M., Vukojević, J. B., Veljović-Jovanović, S. D.,& Duletić-Laušević, S. N.. (2010). Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum. in Bioresources, 5(4).
https://hdl.handle.net/21.15107/rcub_ibiss_1407
Simonić J, Stajić MM, Kukavica BM, Vukojević JB, Veljović-Jovanović SD, Duletić-Laušević SN. Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum. in Bioresources. 2010;5(4):null-2373.
https://hdl.handle.net/21.15107/rcub_ibiss_1407 .
Simonić, Jasmina, Stajić, Mirjana M, Kukavica, Biljana M, Vukojević, Jelena B., Veljović-Jovanović, Sonja D, Duletić-Laušević, Sonja N., "Wheat Straw Conversion By Enzymatic System of Ganoderma Lucidum" in Bioresources, 5, no. 4 (2010),
https://hdl.handle.net/21.15107/rcub_ibiss_1407 .