Abstract
1. The name ;glutathione S-aralkyltransferase' is proposed for the enzyme catalysing the reaction of benzyl chloride with GSH. 2. Results from heat-inactivation studies, ammonium sulphate-fractionation and acid-precipitation experiments, and studies of the distribution of activities in rat liver, in rat kidney and in the livers of other animals indicate that glutathione S-aralkyltransferase differs from glutathione S-alkyltransferase, S-aryltransferase, S-epoxidetransferase and an S-alkenetransferase. 3. The distribution of these enzymes in the livers of the animal species examined was different. 4. Glutathione S-alkyltransferase, S-aralkyltransferase and the S-alkenetransferase that are present in rat liver supernatant were inhibited by GSSG, and the nature of the inhibition varied in each case. 5. 3,5-Di-tert.-butyl-4-hydroxybenzyl acetate reacts spontaneously with GSH, but the rat liver-supernatant-catalysed reaction of GSH with this and other aralkyl esters was weak. 6. A probable function of the glutathione S-transferases is the protection of cellular constituents from strong electrophilic agents.