Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver.
The cytoplasmic NADPH-dependent prostaglandin D2 11-keto reductase from rabbit liver was purified by a series of chromatographic procedures including isoelectric focusing. The enzyme catalyzed the conversion of prostaglandin D2 to prostaglandin F2 alpha and had a pH optimum of 7.0-7.5, and an isoelectric point of 5.8. The molecular weight was estimated to be 66 000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymic activity was time and concentration dependent and required NADPH as cofactor.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D006911:Hydroxyprostaglandin Dehydrogenases / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology*; D008297:Male; D009249:NADP / Q000378:metabolism; D010974:Platelet Aggregation / Q000187:drug effects; D011457:Prostaglandins D / Q000378:metabolism; D011460:Prostaglandins F / Q000378:metabolism; D011817:Rabbits
D011457:Prostaglandins D; D011460:Prostaglandins F; D009249:NADP; D006911:Hydroxyprostaglandin Dehydrogenases; C031051:prostaglandin-F synthase