Penning T M, Sharp R B
Department of Pharmacology, University of Pennsylvania, School of Medicine, Philadelphia 19104-6084.
Biochem Biophys Res Commun. 1987 Oct 29;148(2):646-52. doi: 10.1016/0006-291x(87)90925-9.
Homogeneous 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from rat liver cytosol displays 9, 11, and 15-hydroxyprostaglandin dehydrogenase activity. Using [14C]-PGF2 alpha as substrate the products of this reaction were separated by TLC and identified by autoradiography as PGE2 and PGB2. The purified enzyme catalyzes this reaction at a rate 200 times faster than cytosol. This corresponds to the rate enhancement observed when the enzyme is purified from cytosol using androsterone (a 3 alpha-hydroxysteroid) as substrate and suggests that it may represent a major 9-hydroxyprostaglandin dehydrogenase in this tissue. Although the 3 alpha-HSD has many properties in common with the 9-hydroxyprostaglandin dehydrogenase of rat kidney, rat kidney contains no protein that is immunodetectable with polyclonal antibody raised against the purified 3 alpha-HSD.
来自大鼠肝脏胞质溶胶的均一3α-羟基类固醇脱氢酶（3α-HSD）具有9、11和15-羟基前列腺素脱氢酶活性。以[14C]-PGF2α为底物，该反应的产物通过薄层层析进行分离，并通过放射自显影鉴定为PGE2和PGB2。纯化后的酶催化该反应的速率比胞质溶胶快200倍。这与使用雄甾酮（一种3α-羟基类固醇）作为底物从胞质溶胶中纯化该酶时观察到的速率增强相对应，表明它可能是该组织中主要的9-羟基前列腺素脱氢酶。尽管3α-HSD与大鼠肾脏的9-羟基前列腺素脱氢酶有许多共同特性，但大鼠肾脏中不存在能用针对纯化的3α-HSD产生的多克隆抗体免疫检测到的蛋白质。
