Groman E V, Engel L L
Biochim Biophys Acta. 1977 Dec 8;485(2):249-54. doi: 10.1016/0005-2744(77)90161-9.
When a crude extract of Pseudomonas testosteroni induced with testosterone was subjected to polyacrylamide gel electrophoresis, six bands that stained for 17 beta-hydroxysteroid dehydrogenase activity was 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) beta-hydroxysteroid dehydrogenase (EC 1.1.1.51) in its chromatography properties on DEAE-cellulose, substrate and cofactor specificity, immunological properties and heat stability. The preparation appears devoid of 3alpha-, 3beta-, 11beta-, 17alpha-, 20alpha-, and 20beta-hydroxysteroid dehydrogenase activities. The enzyme transfers th 4-pro-S-hydrogen of NADH from estradiol-17beta (1,3,5(10)estratriene-3,17beta-diol) to estrone (3-hydroxy-1,3,5(10)-estratriene-17-one).
用睾酮诱导的睾丸酮假单胞菌粗提物进行聚丙烯酰胺凝胶电泳时,观察到有六条带呈现17β - 羟基类固醇脱氢酶活性。已获得一种蛋白质组分,它含有与迁移速度最快的条带相对应的酶,且不具有其他羟基类固醇脱氢酶活性。该制剂在DEAE - 纤维素上的色谱性质、底物和辅因子特异性、免疫学性质以及热稳定性方面,似乎与先前分离的3(17)β - 羟基类固醇脱氢酶(EC 1.1.1.51)不同。该制剂似乎不具有3α -、3β -、11β -、17α -、20α - 和20β - 羟基类固醇脱氢酶活性。该酶将NADH的4 - pro - S - 氢从雌二醇 - 17β(1,3,5(10) - 雌三烯 - 3,17β - 二醇)转移至雌酮(3 - 羟基 - 1,3,5(10) - 雌三烯 - 17 - 酮)。