Kitamura S, Katsura H, Tatsumi K
Institute of Pharmaceutical Science, Hiroshima University, School of Medicine, Japan.
Biochem Mol Biol Int. 1993 Aug;30(5):839-47.
A 15-ketoprostaglandin delta 13-reductase was purified to homogeneity from rat liver. The enzyme used NADPH much more effectively than NADH as an electron donor. The molecular weight was estimated to be 39,500 by electrophoresis and 42,000 by gel filtration. The Km apparent for 15-ketoprostaglandin F2 alpha was 213 nM. The enzyme was markedly inhibited by dicumarol, quercitrin, p-chloromercuribenzoic acid and indomethacin. The enzyme had an isoelectric point at pH 4.5 and a broad pH optimum. The enzyme also exhibited the double bond reductase activity toward several xenobiotics with the double bond adjacent to the carbonyl group.
从大鼠肝脏中纯化出一种15-酮前列腺素δ13-还原酶，使其达到同质状态。该酶作为电子供体时，使用NADPH比使用NADH更有效。通过电泳估计其分子量为39,500，通过凝胶过滤估计为42,000。15-酮前列腺素F2α的表观Km值为213 nM。该酶受到双香豆素、槲皮苷、对氯汞苯甲酸和吲哚美辛的显著抑制。该酶的等电点为pH 4.5，具有较宽的最适pH值。该酶还对几种羰基相邻带有双键的外源化合物表现出双键还原酶活性。
