Kung-Chao D T, Tai H H
Biochim Biophys Acta. 1980 Jul 10;614(1):1-13. doi: 10.1016/0005-2744(80)90161-8.
The cytoplasmic NAD+-dependent 15-hydroxyprostaglandin dehydrogenase (11 alpha, 15-dihydroxy-9-oxoprost-13-enoate:NAD+ 15-oxidoreductase, EC 1.1.1.141) from porcine kidney was purified to a specific activity of 1.2 unit per mg protein by a series of chromatographic techniques including affinity chromatography. The native molecular weight of the enzyme was estimated to be 45 000. Substrate specificity studies indicated that the enzyme was NAD+-specific and was able to catabolize readily various prostaglandins, with the exception of prostaglandin B and thromboxane B. The enzyme was inhibited by sulfhydryl inhibitors, diuretic drugs and various fatty acids.
通过包括亲和色谱在内的一系列色谱技术,从猪肾中纯化出细胞质烟酰胺腺嘌呤二核苷酸(NAD⁺)依赖性15-羟基前列腺素脱氢酶(11α,15-二羟基-9-氧代前列腺-13-烯酸:NAD⁺ 15-氧化还原酶,EC 1.1.1.141),其比活性达到每毫克蛋白质1.2单位。该酶的天然分子量估计为45000。底物特异性研究表明,该酶对NAD⁺具有特异性,并且能够轻易分解各种前列腺素,但前列腺素B和血栓素B除外。该酶受到巯基抑制剂、利尿药和各种脂肪酸的抑制。