Abstract
We have purified a cytochrome P-450 from microsomes of pig adrenal glands to homogeneity (11.1 n moles heme/mg protein) as demonstrated by electrophoresis on polyacrylamide gels with sodium dodecyl SO 4 and by line of identity with an antibody using double diffusion. The enzyme shows both 17α-hydroxylase and C 17,20-lyase activities and therefore constitutes a C 21 side-chain cleavage system like that previously purified in this laboratory from neonatal pig testis. Antibody to the testicular enzyme cross-reacts (line of identity) with both enzymes. It is concluded that the adrenal enzyme is the same or very similar to the testicular enzyme, that each enzyme possesses two enzymatic activities, and that microsomes provide some regulatory device to limit the lyase activity of the enzyme in vivo . No evidence was found for the usually accepted existence of an adrenal steroid 17α-hydroxylase without lyase activity.
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