NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from porcine kidney. I. Purification and partial characterization.
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.
D000818:Animals; D004232:Diuretics / Q000494:pharmacology; D006911:Hydroxyprostaglandin Dehydrogenases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D007668:Kidney / Q000201:enzymology*; D008970:Molecular Weight; D009243:NAD / Q000494:pharmacology; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013552:Swine
D004232:Diuretics; D013439:Sulfhydryl Reagents; D009243:NAD; D006911:Hydroxyprostaglandin Dehydrogenases