1. 2-Chloro-1-(2,4,5-trichlorophenyl)vinyl dimethyl phosphate (tetrachlorvinphos) is demethylated by mammalian liver supernatant (100000g) protein in the presence of GSH. 2. GSH acts as an acceptor of the transferred methyl group to form S-methyl glutathione. 3. The enzyme that catalyses this reaction is present in the soluble fraction of liver from mouse, rat, rabbit and pig at similar activity. The enzyme was purified 45-fold from pig liver, dimethyl 1-naphthyl phosphate being used as assay substrate. 4. Methyl groups are readily removed from most of the substrates studied; ethyl groups are removed at one-fiftieth to one-hundredth of the rate for methyl groups. It is likely that the enzyme plays an important role in the detoxification of the phosphate triester pesticides containing CH3–O–P groups.
Phosphoric acid triester–glutathione alkyltransferase. A mechanism for the detoxification of dimethyl phosphate triesters
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D. H. Hutson, B. A. Pickering, C. Donninger; Phosphoric acid triester–glutathione alkyltransferase. A mechanism for the detoxification of dimethyl phosphate triesters. Biochem J 1 March 1972; 127 (1): 285–293. doi: https://doi.org/10.1042/bj1270285
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