人胎盘15-羟基前列腺素脱氢酶的分离纯化

Isolation and Purification of a NAD^+ -dependent 15-hydroxyprostaglandin Dehydrogenase from Human Placenta

作者从人胎盘分离纯化依赖NAD的15-羟基前列腺素脱氢酶,纯化9300倍以上,收率为9.3％,比活性为6470.60nmol/min·mg,PAGE显示为单带,SDS-PAGE为两带,测得其分子量分别为26和52kd,经Western Blot分析、此两带皆能为该酶的多克隆和单克隆抗体识别。认为此酶由两条分子量相同的亚基组成。

A NAD^+ -dependent 15-hydroxyprostaglandin dehydrogenase hasbeen isolated and purified from humanplacenta About 9300-fold enrichment wasachieved with a yield of 9.3%. The spe-cific activity of the purified enzyme was6470 nmol/min.mg. 15-OH-PGDH showeda single band on PAGE and two bands onSDS-PAGE. The molecular weights wereapproximately 26 and 52 kd, respectively.The two bands were recognized by bothpolycloning and monocloning antibodies ofthe enzyme. It is suggested that the 15-OH-PGDH be composed of two identicalsubunits.