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Activity of Supra (E)-Dependent Dehydrogenases of Staphylococcus epidermidis Strains Susceptible to Cefotaxime

Abstract

Investigation of the activity of supra- and supra (e)-dependent dehydrogenases of the Staphylococcus epidermidis strains isolated from the pharynx mucous membrane of healthy subjects showed that the level of the substrate exchange between the tricarbonic acid cycle and the amino acid metabolism reactions, as well as the intensity of the glycolysis terminal reactions and the glutathione reductase activity depended on the bacteria susceptibility to cefotaxime.

About the Authors

O. A. Kolenchukova
Research Institute of the North Medical Problems, Siberian Department of the Russian Academy of Medical Sciences, Krasnoyarsk; Siberian Federal University, Krasnoyarsk
Russian Federation


A. A. Savchenko
Research Institute of the North Medical Problems, Siberian Department of the Russian Academy of Medical Sciences, Krasnoyarsk; Siberian Federal University, Krasnoyarsk
Russian Federation


References

1. Березин А. Г., Ромашов О. М., Яковлев С. В. Характеристика и клиническое изучение бета-лактамаз расширенного спектра. Антибиотики и химиотер 2003; 7: 3-9.

2. Булгакова В. Г., Орлова Т. И., Грушина В. А. Изучение штамма Staphylococcus aureus, устойчивого к актиномицину D. Там же; 2000; 8: 6-11.

3. Винников А. И., Бабенко Ю. С. Особенности гликолиза и пентозофосфатного пути у чувствительных и устойчивых к новобиоцину стафилококков. Там же; 1989; 34: 1: 34-37.

4. Бабенко Ю. С., Орябинская Л. Б. Ферментативный лизис клеток стафилококка и получение клеточных стенок. Там же; 1988; 33: 2: 110-115.

5. Савченко А. А. Биолюминесцентное определение активности НАД- и НАДФ-зависимых глутаматдегидрогеназ лимфоцитов. Лаб дело 1991; 11: 22-25.

6. Тюлькова Н. А., Антонова Э. В. НАД(Ф)Н-реагент для биолюминесцентного анализа. Красноярск: ИБФ, 1991; 18.

7. Берёзов Т. Т., Коровкин Б. Ф. Биологическая химия. М.: 1998; 704.

8. Branduardi P. P., Sauer M. M., De Gioia L. L. et al. Lactate production yield from engineered yeasts is dependent on the host background, the lactate dehydrogenase source and the lactate export. Microbiol Cell Fact 2006; 5: 1: 4.

9. Rosario C. J., Bender R. A. Importance of tetramer formation by the nitrogen assimilation control protein for strong repression of glutamate dehydrogenase formation in Klebsiella pneumoniae. J Bacteriol 2005; 187: 24: 8291-8299.

10. Tanous C., Chambellon E., Le Bars D. et al. Glutamate dehydrogenase activity can be transmitted naturally to Lactococcus lactis strains to stimulate amino acid conversion to aroma compounds. Appl Environ Microbiol 2006; 72: 2: 1402-1409.

11. Shoemark D. K., Cliff M. J., Sessions R. B., Clarke A. R. Enzymatic properties of the lactate dehydrogenase enzyme from Plasmodium falciparum. FEBS J 2007; 274: 11: 2738-2748.

12. Van Cao T., Lambert D. O., Nhu H. K. Distribution of extended-spectrum /З-lactamases in clinical isolates of Enterobacteriaceae in Vietnam. Antimicrob Agents Chemother 2002; 46: 12: 3739-3743.


Review

For citations:


Kolenchukova O.A., Savchenko A.A. Activity of Supra (E)-Dependent Dehydrogenases of Staphylococcus epidermidis Strains Susceptible to Cefotaxime. Antibiot Khimioter = Antibiotics and Chemotherapy. 2009;54(5-6):13-15. (In Russ.)

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ISSN 0235-2990 (Print)