Abstract
We examined the in vitro shuttle metabolism between dihydrotestosterone (DHT) and 5α-androstane-3α,17β-diol (3α-diol) by 3α-hydroxysteroid dehydrogenase (3α-HSD, E.C. 1.1.1.50) in rat submandibular gland (SMG) and ventral prostate (VP). The protein having molecular weight of 30 kDa, which was revealed by Sephacryl S-200 column chromatography, had 3α-HSD activity to produce 3α-diol from DHT, and also showed an oxidative 3α-HSD (3α-HSDO) ability to produce DHT from 3α-diol. From the kinetic studies, the apparent K m and V max values of 3α-HSD for DHT and NADPH were 6.4 μM, 1429 pmol/mg protein per min and 33.0 μM, 1205 pmol in SMG, and 9.3 μM, 377 pmol and 34.0 μM, 192 pmol in VP. The corresponding values of 3α-HSDO for 3α-diol and NADP + were 18.0 μM, 714 pmol and 14.0 μM, 445 pmol in SMG, and 14.0 μM, 417 pmol and 36.0 μM, 77 pmol in VP. The affinities for DHT and 3α-diol and the cosubstrate requirements of this enzyme in SMG were similar to those in VP. However, higher capacities of 3α-HSD and 3α-HSDO in SMG than in VP were shown. This suggests that there may be more 3α-HSD in the SMG.
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