Abstract
When a crude extract of Pseudomonas testosteroni induced with testosterone was subjected to polyacrylamide gel electrophoresis, six bands that stained for 17β-hydroxysteroid dehydrogenase activity were observed. A protein fraction containing the enzyme corresponding to the fastest migrating band and devoid of the other hydroxysteroid dehydrogenase activities has been obtained. This preparation appears to be distinct from the previously isolated 3(17)β-hydroxysteroid dehydrogenase (EC 1.1.1.51) in its chromatographic properties on DEAE-cellulose, substrate and cofactor specificity, immunological properties and heat stability. The preparation appears devoid of 3α-, 3β-, 11β-, 17α-, 20α-, and 20β-hydroxysteroid dehydrogenase activities. The enzyme transfers the 4-pro-S-hydrogen of NADH from estradiol-17β (1,3,5,(10)estratriene-3,17β-diol) to esterone (3-hydroxyl-1,3,5(10)-estratriene-17-one).
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