[Effect of various storage methods on the viability of myxobacteria].

Viability of myxobacteria strains Myxococcus xanthus UNCM 10041, Polyangium cellulosum UNCM 10043, Archangium gephyra UNCM 10001 stored by the methods of lyophilization, cryoconservation, drying on paper discs, suspending in distilled water or physiological solution under a layer of mineral oil. The best results on viability preservation of all three studied strains were obtained when using the method of cryoconservation. It has been shown that the strains M.

[Effect of DDT on the interaction of cortisol with glucocorticoid-binding proteins in rat brain].

It was established that DDT is the isosteric inhibitor of cortisol interaction with purified rat brain glucocorticoid-binding proteins. These results were confirmed in the experiments in vivo on Vistar female rats from one generation.

[Degradation of 4,9-dichlorodibenzodioxin in rat liver microsomes].

The rat liver microsomal cytochrome P 450 was established to dechlorinate 4,9-dichlorodibenzodioxin into 4,9-dihydroxydibenzodioxin. Two isoforms of this cytochrome P 450 were electrophoreticaly identified and quantified. 4,9-dihydroxidibenzodioxin transforms into resorcin with the help of ascorbic acid.

[Effect of reducing agents-antioxidants on rat uterine aromatase activity in vitro].

The effect of different reductors-antioxidants (ascorbic acid, cysteine, glutathione-SH and hydroquinone) on purified rat uterine aromatase activity was studied. It was established that all these compounds were aromatase activators. The possible mechanisms of this activation were discussed.

[Effect of some antioxidants and caffeine on xanthine dehydrogenase activity in rat liver in vitro].

The regulation of xanthine dehydrogenase activity by reductors-antioxidants (ascorbic acid, glutatione-SH, gentathione dithiothreitol, cysteine and hydrocortisone) and caffeine was investigated in the purified enzymatic preparation in vitro. It was shown, that reductors-antioxidants were incompetitor inhibitors of xanthine dehydrogenase and caffeine was a competitor-inhibitor of it. The mechanisms of inhibition of xanthine dehydrogenase activity by these agents were discussed.

[In vitro study of regulation of rat liver xanthine oxidase activity by antioxidant reducing agents].

It was learned the regulation of xanthine oxidase activity from rat liver in the partly purified prepared by ascorbic acid, glutathione-SH, dithiothreitol, cysteine++ and hydrocortisone++. It was shown that ascorbic acid glutathione-SH, dithiothreitol, and cysteine++ can be activators and uncompetitor inhibitors of xanthine oxidase in dependence from concentration. As far as hydrocortisone is concerned, it is a powerful uncompetitor inhibitor of xanthine oxidase, that is bind with it.

[Effect of caffeine on xanthine oxidase activity].

The effect of caffeine on the xanthine oxidase activity in human organism has been studied. It was revealed that caffeine calls the inconsiderable reliable increase of the level of uric acid and the reliable lowering of levels of hypoxanthine and xanthine in urine. The isosteric inhibition of xanthine oxidase activity by caffeine was revealed in the experiments in vitro.