ROLE OF GLUTATHIONETRANSFERASE AND GLUTATHIONE-DEGRADING ENZYMES IN A METABOLISM OF DI-(2-CHLOROETHYL)-SULFIDE FOR RATS

Boitsova L.V.

The effects of di-(2-chloroethyl)-sulfide administered at a 1/2 LD₅₀ single dose on reduced glutathione level as well as glutathione transferase, g-glutamyltranspeptidase, peptidase, aminopeptidase M, and b-lyase activities in rat liver and kidneys were studied.

It was shown that cytotoxic effects of an alkylating agent preparation reduced glutathione level in the studied liver cells in the earlier period of intoxication (15 min, 3, 6 hours) with the consequent compensatory increase from 24 hours. During 30 minutes just after the introducing of alkylating agent, the activity of g-glutamyltranspeptidase, and b-lyase has depressed. Di-(2-chloroethyl)-sulfide produced a sustained enhancement of the activity II of a phase enzymes of detoxification, namely glutathione transferase with further increase of processes of a catabolism of glutathione and conjugation with glutathione. The last ones are connected to operation of glutathione-degrading enzymes — g-glutamyltranspeptidase, peptidase, aminopeptidase M of kidney microvillis brush border membranes.

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