Abstract
Rabbit liver microsomes were shown to contain enzyme systems that converted heptachlor, aldrin, and isodrin into their corresponding epoxides. No other metabolites were produced. The epoxidases required NADPH 2 and oxygen. Epoxidation of heptachlor and aldrin was inhibited by SKF 525-A, piperonyl butoxide, parathion, and γ-BHC. Mutual inhibition between the two substrates as well as inhibition by epoxides was observed. Epoxidase activities were also found in rat liver microsomes and in insect homogenates. A model hydroxylation system (EDTA, Fe 2+, and ascorbate) did not simulate microsomal epoxidase. Metabolism of γ- and δ-pentachlorocyclohexene was similarly demonstrated with rabbit liver microsomes.
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