NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from porcine kidney. I. Purification and partial...

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.