Abstract
Hepatic estradiol-17 beta dehydrogenase from chickens catalyzed the reduction of the 3-keto group of androgens such as 5 alpha-dihydrotestosterone and 5 alpha-androstane-3,17-dione as well as the 17-keto reduction of 4-androstene-3,17-dione and dehydroepiandrosterone. The reaction products from 17-ketosteroid and 3-ketosteroid substrates were identified as 17 beta-hydroxysteroids and 3 beta-hydroxysteroids, respectively, by thin layer chromatography, high performance liquid chromatography and gas chromatography. Barbital inhibited both 17 beta-estradiol dehydrogenase and 5 alpha-androstane-3,17-dione reductase activity noncompetitively giving the same kinetic constant, Ki = 50 microM. 5 alpha-Androstane-3,17-dione competitively inhibited 17 beta-estradiol dehydrogenase activity. These results indicate that chicken liver estradiol-17 beta dehydrogenase is in fact a 3 beta- and 17 beta-hydroxysteroid dehydrogenase and that both 3- and 17-ketosteroids bind to the same catalytic site.
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