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. 1973 Apr;131(4):765–769. doi: 10.1042/bj1310765

Distribution of enzymes that catalyse reactions of glutathione with αβ-unsaturated compounds

L F Chasseaud 1,*
PMCID: PMC1177536  PMID: 4722451

Abstract

1. A study of the distribution of glutathione S-alkenetransferases in the livers of vertebrate species suggests that different enzymes may catalyse reactions of GSH with (i) trans-benzylideneacetone, (ii) 2,3-dimethyl-4(2-methylenebutyryl)phenoxyacetic acid, (iii) cinnamonitrile, (iv) o-chlorobenzylidenemalononitrile, (v) methyl vinyl sulphone, and (vi) 3-(β-nitrovinyl)indole. 2. Glutathione S-alkenetransferase activity was generally greatest in rat liver, but the enzyme in hamster liver was more active towards o-chlorobenzylidenemalononitrile, and the enzyme in rabbit, hamster, guinea-pig and mouse livers was more active towards methyl vinyl sulphone. 3. Results from studies of the distribution of activities in rat liver and rat kidney, heat inactivation of rat liver supernatants, and (NH4)2SO4 fractionation and acid-precipitation experiments, differentiated further between some of the enzymes concerned with substrates (i)–(vi). 4. The infrequent detection of mercapturic acids in vivo is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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