[Activity of enzymes of ethanol metabolism as a test in evaluating the effectiveness of sensitizing alcohol deterrents].

A procedure is developed for determination of the efficiency of the antialcoholic drugs' action on the system of ethanol oxidation in vitro: alcohol dehydrogenase by the direct and reverse reactions and aldehyde dehydrogenase of subcellular fractions of the rat liver. This procedure is also used to determine the antialcoholic activity of a number of new compounds and to compare them with disulphiram (antabus, teturam), the known antialcoholic drug.

[Disulfiram inhibition of aldehyde reductase from the rat liver].

Disulphiram (tetraethylthiuram disulphide teturam, antabus), the known antialcoholic preparation, is studied for its effect on the aldehyde reductase activity (EC 1.1.1.

[Aldehyde dehydrogenases in the rat liver after implantation of a prolonged-action preparation of an alcohol deterrent].

Activity of aldehyde dehydrogenase isoenzymes was studied in rat liver mitochondria and microsomes after implantation of the new antialcohol drug of the long-term effect synthesized on the basis of disulphirame. Disulphirame, both in vivo and in vitro was shown to inhibit dissimilarly these isoenzymes. The degree of sensitivity of various aldehyde dehydrogenase isoenzymes to disulphirame is important for estimation of the drug efficiency.

[Effect of SH-reagents on aldehyde dehydrogenase activity of the rat liver].

SH-reagents: tetraethylthiuram disulphide (TETD), 5,5'-dithiobisnitrobenzoic acid (DTNB), p-chloromercurybenzoate (p-ChMB), N-ethylmaleimide (NEM) were studied for their effect on the aldehyde dehydrogenase activity of mitochondrion (isoenzymes I and II) and microsome (isoenzyme II) fractions of the rat liver. TETD is established to inhibit isoenzyme I and isoenzyme II activity of mitochondrial aldehyde dehydrogenase by 100 and 50%, respectively, and the microsomal enzyme activity by 20%. DTNB and NEM inhibit 30-50% of the activity in two isoforms of mitochondrial aldehyde dehydrogenase having no effect on the enzymic activity in microsomes; p-ChMB inhibits completely the activity of the enzyme under study both in the mitochondrial and microsomal fractions.

[Activity of proteolytic enzymes in the kidney and blood serum of rabbits during implantation of different polyurethanes].

It is shown that the activity of neutral proteinase both in homogenate and in blood serum increases by the 14th day the D-1 sample being implanted. In the subsequent periods after implantation the enzyme activity in homogenate is the same. Three and six months after implantation the neutral proteinase activity in blood serum decreases as compared to the norm.