Bìol. Tvarin, 2016, volume 18, issue 2, pp. 9–17


N. О. Bodnarchuk, SMMandzynets, LIPetrukh, DISanagurski


Ivan Franko National University of Lviv,
4 Hrushevskogo
str., Lviv 79005, Ukraine, This email address is being protected from spambots. You need JavaScript enabled to view it.

The aim of this work was to study the influence of Flurenizide (antibiotic of antimicrobial, antituberculous, antichlamydia, immunomodulator, antioxidant, hepatoprotective, antiinflammatory, antiviral action) on the antioxidant homoeostasis of loach embryos (Misgurnus fossilis L.) during early embryogenesis.The superoxide dismutase and catalase activity under the action of Flurenizide in concentrations 0,01; 0,05; 0,15; 1; 5; 15 mM of loach embryos at the stage of development first (2 blastodmeres), fourth (16 blastodmeres), sixth (64 blastodmeres), eighth (256 blastodmeres), tenth (1024 blastodmeres) crushing zygote was investigated. The twofactor analysis of variance was conducted to expose the level of influence of Flurenizide action, time of development and untaken into account factors on activity of the investigated enzymes.

It is established that Flurenizide violates the work of superoxiddysmutase on all stages of loach embryos development. It predetermines the slump of activity of this enzyme on the stage of development 16 blastodmeres. It is revealed that the investigated antibiotic in concentrations 1; 5; 15 mМ on the stage of the 10th division of bioblasts predetermines the slump of activity of superoxiddysmutase, while in the concentrations of 0,01mМ and 0,05 mМ Flurenizide causes the increase of this enzyme activity.

It is validified that Flurenizide in all investigated concentrations causes the slump of catalase activity on the stage of 64 blastodmeres of loach embryos development. On the stage of the 10th loach embryos division Misgurnus fossilis L. Flurenizide in the concentrations of 0,01 mМ and 0,05 mМ predetermines the considerable increase of catalase activity and in the higher concentrations of 1 mМ and 15 mМ conduces to the slump of activity of the investigated enzyme.

By means of twofactor analysis of variance it is established that the powerful influence on superoxide dismutase and catalase activity of loach the embryos is rendered by the untaken into account factors. Flurenizide carries out a mediocre influence on work of these enzymes which testifies probably the indirect action of this factor on activity of SOD and CAT. It is established that time of development has more expressed influence on catalase activity.


1. Belenichev I. F., Levytski E. L., Gubski J. I. Antioxidant system of defence of organism. Modern problems of toxicology, 2002, no. 3, pp. 24–36. (in Ukrainian)
2. Pshechenko N. V., Bondarenko V. A., Mareshina T. A. Correction of the antioxidation system preparation of liposome as method of treatment of infectious diseases. Biolog. Announcer, 2001, vol. 5, no. 1–2, pp. 64–67. (in Ukrainian)
3. Gryshchenko V. A. Intensity of lipoperoxidase and state of the antioxidant system of defence for calves, to have had on dyspepsia. The Ukr. Biochem. J., 2004, vol. 76, no. 5, pp. 102–106. (in Ukrainian)
4. Heletiy E. M. Influence of preparation of dystonol on the state of the phermentative system of antioxidant defence of organism of pheasants. Sciences. announcer Lviv national academy veterinary medicine the named after S. Z. Gzhytsky, 2006, vol. 8, no. 2 (29), P. 2, pp. 27–31. (in Ukrainian)
5. Hlogyk I., Snitynski V., Iskra R. Activity of the antioxidant system for ruminant animals depending on the physiology state. Announcer of the Lviv university, Biological Series, 2002, Is. 31, pp. 256–260. (in Ukrainian)
6. Burlaca A. P., Sydoryk E. P., Drugyna N. A. Kinetic conformities to law of activity of the fermentative antioxidative systems in organs at chemical kancerogenesis of mammary glands and liver. Dop. NAN of Ukraine, 1998, no. 11, pp. 177–181. (in Ukrainian)
7. Lai C. C., Huand W., Askari A. Differential regulation of superoxide dismutase in copper deficient rat organs. Free Radic. Biol. and Med, 1994, vol. 16, pp. 613–620. https://doi.org/10.1016/0891-5849(94)90061-2
8. Lane D. P. Guardian of the genom. Nature, 1992, vol. 358, no. 141, pp. 15–16. https://doi.org/10.1038/358015a0
9. Lowry O. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 1951, vol. 193, no. 1, pp. 404–415.
10. Matsopa I. V., Grygoryeva N. P., Meshchyshyn I. F. Adaptation of the antioxidant system of kidneys of rats to the different light modes for intoxications by a tetrachloromethane and actions of melatonin. The Ukr. Biochem. J., 2010, vol. 82, no. 2, pp. 75–84. (in Ukrainian)
11. Mihalik O. Modern drugs for chemotherapy of viral infections: a guide. Lviv, 2013, 180 p. (in Ukrainian)
12. Neyfah A., Timofeeva M. Problems in molecular biology regulation development. Moscow, Nauka, 1978, 336 p. (in Russian)
13. Petrukh L. Fluorene as tuberculostatisc. In: Flurenizide: microbiological, farmacological and clinical aspects, 2008, pp. 464–469. (in Ukrainian)
14. Petrukh L. Flurenizide in veterinary practice. Coll. materials of international scientific-practical conference “Modern problems of veterinary medicine, zooengineering animal products and technologies”, 1997, pp. 216–217. (in Ukrainian)
15. Petrukh L. Pharmaceutical education and language. The achievements of pharmaceutical research, 2011, 152 p. (in Ukrainian)
16. Petrukh L. The urgency of the creation and implementation of industrial production of new medicines. Collection of descriptions of inventions, 2003, 198 p. (in Ukrainian)
17. Petrukh L. Urgency creation and implementation in the industrial production of new drugs. Collection of descriptions of inventions, Lviv, 2003, 196 p. (in Ukrainian)
18. Poberezkina N. B., Losynska N. F. Biological role of superoxiddesmutase. The Ukr. Biochem. J., 1989, vol. 61, no. 2, pp. 14–21. (in Ukrainian)
19. Abrahamovych O. O., Hrabovska O. I., Terletska O. I. Processes of lipid peroxidation at the chronic defeats of liver. Medical chemistry, 2000, vol. 2, no. 1, pp. 5–8. (in Ukrainian)
20. Golovchak N. P., Tarnovska A. V., Kotsumbas H. I., Sanagurski D. I. Processes of peroxide of lipids in living organisms: monography. Lviv, LNU named after Ivan Franko, 2012.
21. Ratych I. B., Martynuk U. A. To the kind and organ-tissue features of antioxidant status for the birds. Sciences. announcer Lviv. national academy veterinary medicine named after S. Z. Gzhytsky, 2006, vol. 8, no. 2 (29), pp. 2, pp. 125–130. (in Ukrainian)
22. Kleveta H., Chaika Y., Starykovych L., Vyhovska T. Research of separate enzymes of the antioxidant system of enterocytes of thin bowels of rats at the terms of lowintensive of the X-rayed irradiation. Announcer of the Lviv university, Biological Series, 2002, is. 29, pp. 39–45. (in Ukrainian)
23. Sanagurskiy D. I. Biophysics objects. Lviv, Publishing House of Ivan Franko LNU, 2008, 522 p. (in Ukrainian)
24. Tarnovska A. V., Otchych V. P., Sanagurski D. I. Superoxiddysmutase and katalase activity in the embryos loach at influence of flumikvil. Experimental and clinical physiology and biochemistry, 2006, no. 4 (36), pp. 7–10. (in Ukrainian)
25. Yablonska S., Filinska O., Lynchak O., Ostrovska G. Liver’s damage and glutathione antioxidant system after treatment with the colon carcinogen 1,2-dimethylhydrazine and novel cytostatic maleimide derivative. The Ukr. Biochem. J, VII Parnas Conference, 2009, vol. 81, no. 4, pp. 275. (in Ukrainian)
26. Yablonska S. V., Filinska O. M., Ostrovska H. V. An estimation of hepatotoxicity of new derivative maleimide with cytostatic activity and its influence on peroxide oxidization and antioxidant system of liver. The Ukr. Biochem. J., 2009, vol. 81, no. 5, pp. 83–92. (in Ukrainian)
27. Zyn A., Golovchak N., Sanagurski D. Oxidizing modification of proteins loach embryos Misgurnus fossilis L. during embryogenesis for the actions of hypochlorite of natrium. Announcer of the Lviv university, Biological Series, 2013, is. 61, pp. 11–19. (in Ukrainian)
28. Zyn A. R., Mandzynets S. M, Golovchak N. P., Bura M. V., Sanagurski D. I. Activity of Na+, K+-ATP-aze membranes of embryos loach during early embryogenesis for the actions of hypochlorite of natrium. Biological studies, 2011, vol. 5 (3), pp. 59–66. (in Ukrainian)

Download full text in PDF format




WorldCat Logo