Abstract
Dihydroisodrin is hydroxylated to 6- exo-hydroxy-6,7-dihydroisodrin in southern armyworm gut and vertebrate liver microsomal preparations. The sedimentation characteristics of the hydroxylase, its requirement for NADPH and oxygen, and its inhibition by carbon monoxide and 4,5,6,7-tetrachloro-1,3-benzodioxole indicate that the enzyme system may be classed as a typical microsomal oxidase. The enzyme system is susceptible to substrate inhibition, but in other respects it is similar to microsomal aldrin epoxidase and p-chloro- N-methylaniline demethylase.
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