9-Hydroxyprostaglandin dehydrogenase from rat kidney. Purification to homogeneity and partial characterization.

Abstract

A 9-hydroxyprostaglandin dehydrogenase has been purified from rat kidney to apparent homogeneity. The molecular weight of the enzyme as determined by gel filtration was 33,000. Electrophoresis in sodium dodecyl sulfate gave a value of 34,000 indicating the absence of subunits. The enzyme catalyzes NAD+-specific irreversible oxidation of 15-keto-13,14-dihydro-prostaglandin F2 alpha as well as of 15-keto-PGF2 alpha and PGF2 alpha although at a lesser degree. It does not catalyze the oxidation of 6-keto-PGF1 alpha. The enzyme was sensitive to sulfhydryl inhibitors and was inhibited by prostaglandins, fatty acids, triiodothyroacetic acid, and indomethacin.