Abstract
Dehydrogenation of 5β-androstane-3α,17β-diol to 5β-androstan-3α-ol-17-one was found lo be catalysed by rabbit liver 3-hydroxyhexobarbital dehydrogenase. Rabbit liver cytosol contained several enzyme activities for the dehydrogenation of 5β-androstane-3α, 17β-diol. One of the activities was not separable from 3-hydroxyhexobarbital dehydrogenase in the course of purification and on polyacrylamide gel disc electrophoresis. The activity of 3-hydroxyhexobarbital dehydrogenase was inhibited competitively by 5β-androstane-3α, 17β-diol. Results of a mixed substrate method, thermal inactivation and inhibition by p-chloromercuribenzoate also supported the interpretation that a single enzyme was responsible for the dehydrogenation of 3-hydroxyhexobarbital and 5β-androstane-3α, 17β-diol. It was shown that, in the rabbit liver, 3-hydroxyhexobarbital dehydrogenase was separate from testosterone 17β-dehydrogenase (NADP) (EC 1.1.1.64) by TEAE-cellulose column chromatography, although both enzymes were found to be identical in the case of guinea-pig liver.
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