Abstract
The 5α reductase activity of the monkey epididymis was studied. The enzyme was found in particulate subcellular fractions,its distribution closely resembling that of the microsomal marker enzyme NADPH: cytochrome c reductase, suggesting an association of 5α reductase with membranes of the endoplasmic reticulum. Maximal enzyme activity was found at pH 5.4 and at 32–37 C. The crude nuclear preparation had a Km: 0.315 × 10 −6M and Vmax: 168 pmoles/mg protein/h. The microsomal enzyme had a Km: 0.243 × 10 −6M and Vmax: 828 pmoles/mg protein/h. Neither enzyme preparation was affected by addition to the incubation media of dihydrotestosterone (DHT) or 5α-androstane-3α,17β-diol. The endogenous androgen concentration in the epididymides of 2 different monkeys, in ng/g wet weight was: DHT 20.81 ± 1.98; T: 9.06 ± 2.83; diol: 3.03 ± 0.41.
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