Boutin J A, Shikita M, Talalay P
Biochem Biophys Res Commun. 1986 Mar 28;135(3):795-801. doi: 10.1016/0006-291x(86)90998-8.
Rat liver microsomes contain 3 alpha-hydroxysteroid dehydrogenase (HSD) (EC 1.1.1.50) and dihydrodiol dehydrogenase (DHD) (EC 1.3.1.20) activities. The two enzyme activities were solubilized by 10% Triton X-100 or 0.4% sodium deoxycholate. Unlike the cytosolic enzyme (Penning & Talalay (1983) Proc. Natl. Acad. Sci. U.S.A., 80, 4505), the microsomal HSD and DHD activities were not inhibited by indomethacin. Chromatography of the microsomal Triton X-100 extract on Affigel Blue and then on Phenyl-Sepharose gave an HSD preparation containing no detectable (less than 3 - 5%) DHD activity, whereas chromatography of the deoxycholate extract on Phenyl-Sepharose provided a DHD preparation that lacked measurable HSD activity. These results are in sharp contrast to the cytosolic enzyme where both HSD and DHD activities could be copurified to homogeneity (Penning et al. (1984) Biochem. J. 222, 601).
大鼠肝脏微粒体含有3α-羟基类固醇脱氢酶（HSD）（酶编号1.1.1.50）和二氢二醇脱氢酶（DHD）（酶编号1.3.1.20）活性。这两种酶活性可被10%的 Triton X-100 或 0.4%的脱氧胆酸钠溶解。与胞质酶不同（彭宁和塔拉莱（1983年）《美国国家科学院院刊》，80，4505），微粒体HSD和DHD活性不受吲哚美辛抑制。微粒体Triton X-100提取物先后在Affigel Blue和苯基琼脂糖上进行层析，得到的HSD制剂中未检测到（小于3 - 5%）DHD活性，而脱氧胆酸盐提取物在苯基琼脂糖上进行层析，得到的DHD制剂缺乏可测量的HSD活性。这些结果与胞质酶形成鲜明对比，在胞质酶中，HSD和DHD活性均可共纯化至同质状态（彭宁等人（1984年）《生物化学杂志》222，601）。
