Amet Y, Simon B, Quemener E, Mangin P, Floch H H, Abalain J H
Laboratoire de Biochimie, Faculté de Médecine, CHU Morvan, Brest, France.
J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):689-92. doi: 10.1016/0960-0760(92)90405-8.
3 alpha-Hydroxysteroid dehydrogenase (3 alpha-HSD) activity has been purified to homogeneity, the enzyme is a monomer with a Mw of 32,000 Da. 3 beta-Hydroxysteroid dehydrogenase (3 beta-HSD) activity has been partially purified and has an apparent Mw of 30,000 Da. Both enzymes have the same cofactor requirements, optimal pH. However, 3 beta-HSD appeared to be an integral protein dependent on protein environment for its activity while 3 alpha-HSD activity is a protein more loosely associated to membranes.
3α-羟基类固醇脱氢酶(3α-HSD)活性已被纯化至同质,该酶是一种分子量为32,000道尔顿的单体。3β-羟基类固醇脱氢酶(3β-HSD)活性已被部分纯化,其表观分子量为30,000道尔顿。两种酶具有相同的辅因子需求和最佳pH值。然而,3β-HSD似乎是一种依赖蛋白质环境发挥活性的整合蛋白,而3α-HSD活性是一种与膜结合较松散的蛋白质。