N V Korobeĭnik

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The activity of enzymes, inactivating levomycetin and penicillin in the cells of plague and pseudotuberculosis microbes bearing extrachromosomal determinants resistant to a number of antibiotics was studied as dependent on some cultivation parameters: population age, aeration rate and temperature. It was shown that the highest capacity for levomycetin(More)
Two possible mechanisms of enzymatic inactivation of levomycetin, i.e. acetylation of OH-groups and reduction of the n-nitrophenylic component by the cells and cell-free extracts of V. eltor 2044 with the plasmid or chromosome types of antibiotic resistance were studied in vitro. The vibrio containing the extrachromosome determinants were resistant to a(More)
Purification of chloramphenicol acetyltransferase isolated from the cells of Y. pestis EV-R with extrachromosomal resistance to chloramphenicol included ultrafiltration on the microporous membranes Diaflo-XM 300 and biospecific chromatography on columns with cepharose 4B covalently bound with the reduced chloramphenicol. Elution of chloramphenicol(More)
One of the mechanisms of levomycetin inactivation, i.e. enzymatic acetylation of the plague causative agent and Coli bacteria with chromosomic and episomic type of resistance was studied. It was shown that resistance to levomycetin in the recombinants of the plague microbe and Coli bacteria stipulated by one and the same R-factor was associated with their(More)
A method for fractionation of membrane structures of Yersinia pestis is developed. It involves the following basic stages: the cultivation of bacteria in a liquid nutrient medium, mechanical destruction from the solid state in the X-press or ultrasound treatment of the suspension, subsequent two-stage centrifugation in the step (70-15%) and linear (70-45%)(More)
The authors compared the activity of acetyl-CoA-synthetase and of the enzymes belonging to the group of asparaginic acid in levomycetin sensitive and resistant strains of Y. pestis and E. coli. There were revealed marked differences in the activity of aspartase, fumarase, synthetase and desamidase of L-asparagin, and also of the enzyme activated by acetate(More)
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