Trialkyl phosphorothioates and glutathione S-transferases.

Abstract:

:Using a rat liver cytosol source of enzyme trialkyl phosphorothioates have been shown to be substrates of glutathione S-transferases. Using OSS-trimethyl phosphorodithioate (OSS-Me(O] and OOS-trimethyl phosphorothioate (OOS-Me(O] the methyl transferred to the sulphydryl of glutathione is that attached to phosphorus via an oxygen atom. Fractionation of liver cytosol has shown that although the bulk activity is due to the three isozymes (1-1; 3-4; 1.2), OSS-Me(O) is a general substrate for glutathione S-transferases. The specific activity is low compared with the substrates 1-chloro-2,4-dinitrobenzene and 1,2-dichloro-4-nitrobenzene.

journal_name

Chem Biol Interact

authors

Aldridge WN,Grasdalen H,Aarstad K,Street BW,Norkov T

doi

10.1016/s0009-2797(85)80166-6

subject

Has Abstract

pub_date

1985-07-01 00:00:00

pages

243-56

issue

2

eissn

0009-2797

issn

1872-7786

journal_volume

54

pub_type

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