9-Hydroxyprostaglandin dehydrogenase from rat kidney. Purification to homogeneity and partial characterization.
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.
D000818:Animals; D006911:Hydroxyprostaglandin Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D011453:Prostaglandins / Q000494:pharmacology; D051381:Rats; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D046911:Macromolecular Substances; D011453:Prostaglandins; D006911:Hydroxyprostaglandin Dehydrogenases