Conjugations with glutathione. Distribution of glutathione S-aryltransferase in vertebrate species.

Booth, Boyland & Sims (1961) described and partially purified an enzyme from the soluble supernatant of rat liver which catalyses conjugations of glutathione with aromatic compounds to form thio ethers as a first stage in mercapturic acid biosynthesis, and an apparently similar enzyme has been shown to be involved in processes leading to the biliary excretion of sulphobromophthalein (phenoltetrabromophthaleindisulphonate) conjugates (Combes & Stakelum, 1961). It is suggested that this enzyme, which has previously been called 'glutathiokinase' (Boyland, 1962; Al-Kassab, Boyland & Williams, 1963), should be named 'glutathione S-aryltransferase'. The conjugation of glutathione with aliphatic halogen compounds is catalysed by a liver enzyme that can be separated from that involved in conjugations of glutathione with aromatic compounds (Johnson, 1963). There must therefore be more than one glutathione transferase. The present paper concerns the distribution of the enzyme described by Booth et al. (1961) in several vertebrate species and its apparent identity with the enzyme implicated in biliary sulphobromophthalein excretion.