猴肾二聚体二氢二醇脱氢酶的纯化及部分特性分析

Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney.

作者信息

Hara A, Mouri K, Sawada H

出版信息

Biochem Biophys Res Commun. 1987 Jun 30;145(3):1260-6. doi: 10.1016/0006-291x(87)91573-7.

Abstract

Dihydrodiol dehydrogenase activity was detected in the cytosol of several monkey tissues, among which kidney exhibited the highest activity and contained a high-molecular weight (Mr approximately 65,000) enzyme species. The enzyme species was purified to apparent homogeneity and showed a subunit molecular weight of 39,000. The enzyme oxidized benzene dihydrodiol (Km = 0.9 mM) at a pH optimum of 9.8, and highly reduced vicinal diketones such as camphorquinone (Km = 0.1 mM) and diacetyl (Km = 0.8 mM) around pH 7.5, but alicyclic alcohols, hydroxysteroids and ketosteroids were inactive substrates for this enzyme. Quercitrin, SH-reagents, stilbestrol were inhibitory to the enzyme activity, but other synthetic estrogens, anti-inflammatory agents and 3-ketosteroids were not.

摘要

在几种猴组织的胞质溶胶中检测到二氢二醇脱氢酶活性，其中肾脏的活性最高，且含有一种高分子量（约65,000）的酶种类。该酶种类被纯化至表观均一，其亚基分子量为39,000。该酶在最适pH为9.8时氧化苯二氢二醇（Km = 0.9 mM），并在pH 7.5左右高效还原邻位二酮，如樟脑醌（Km = 0.1 mM）和二乙酰（Km = 0.8 mM），但脂环醇、羟基类固醇和酮类固醇是该酶的无活性底物。槲皮苷、巯基试剂、己烯雌酚对酶活性有抑制作用，但其他合成雌激素、抗炎药和3-酮类固醇则无此作用。