CONJUGATIONS WITH GLUTATHIONE. THE ENZYMIC CONJUGATION OF SOME CHLOROCYCLOHEXENES

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Abstract
[alpha]-3,4,5,6-Tetrachlorocyclohex-1-ene and gamma-2,3,4,5,6-pentachlorocyclohex-1-ene are conjugated with glutathione in vitro by a rat-liver enzyme that is probably glutathione S-aryltransferase. Chlorocyclohexane and the [alpha],[beta] -,gamma-and [delta] -isomers of hexachlorocyclohexane were not substrates for rat-liver glutathione S-aryltransferase. Glutathione-S-aryltransferase activity was present in tissue preparations of houseflies of insecticide-resistant and -susceptible strains. More activity was found in a dieldrin-resistant strain of houseflies fed on dieldrin than in either a dieldrin-resistant strain not fed on dieldrin or a control strain of dieldrin-susceptible houseflies. Housefly soluble supernatant preparations converted S-(2-chloro-4-nitrophenyl)glutathione into the corresponding cysteine and mercapturic acid derivatives.