Metabolism of Benzene Hexachloride Isomers and Related Compounds In Vitro. II. Purification and Stereospecificity of House Fly Enzymes1

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Abstract
Attempts were made to purify the house fly, Musca domestica L., enzymes that metabolize the α- and γ-isomers of 1,2,3,4,5,6-hexachlorocyclohexane (BHC) and the γ- and δ-isomers of 1,3,4,5,6- pentachlorocyclohex -1 - ene (PCCH) to unknown water-soluble substances in the presence of glutathione. Quantitative analyses of effluents from ion exchange columns indicated at least 3 enzyme systems that metabolize both α-BHC and γ-PCCH, with different ratios of metabolizing activity for the 2 substrates. The activity of enzymes from various ages of adult house flies demonstrated enzyme stereospecificity in the metabolism of α- and γ-BHC. The development of enzyme activity with the age of adult flies had no correlation with the lethal dosage of γ-BHC to flies of the same age. No large changes of enzyme activity for metabolism 7-PCCH were found through all stages of metamorphosis, α- and γ-BHC metabolizing enzymes were predominant in the adult stage only. DDT was dehydrochlorinated to DDE (2,2-bis-(pchlorophenyl) -1,1-dichloroethylene) with the enzymatic reaction system used for BHC. Several inhibition studies did not differentiate enzymes causing dehydrochlorination of DDT from those metabolizing BHC.

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