Tanaka T, Kotani T, Ohtaki S, Nagai K, Tsuruta K, Mori N
Biochem Biophys Res Commun. 1986 Mar 28;135(3):1058-63. doi: 10.1016/0006-291x(86)91035-1.
NAD-dependent 15-hydroxyprostaglandin dehydrogenase has been isolated from human term placenta. About 9,000-fold enrichment was achieved with a yield of 7.6%. Electrophoretic analyses suggested that glycerol stabilized an active structure of the enzyme, and sodium dodecyl sulfate might dissociate it. The instability of the enzyme activity may relate to its labile oligomeric structure which is easily dissociated into subunits.
已从足月人胎盘中分离出NAD依赖的15-羟基前列腺素脱氢酶。实现了约9000倍的富集，产率为7.6%。电泳分析表明，甘油可稳定该酶的活性结构，而十二烷基硫酸钠可能使其解离。酶活性的不稳定性可能与其易解离为亚基的不稳定寡聚结构有关。
