Multiple molecular forms of prostaglandin 15-hydroxydehydrogenase and 9-ketoreductase in chicken kidney.

Prostaglandin-15-hydroxydehydrogenase and prostaglandin-9-keto-reductase were purified from chicken kidney. Both enzymes exist in multiple forms as determined by isoelectric focusing. The dehydrogenases catalyze the transformation of the functional group at C-15 but not the functional group at C-9. The preferred cofactors in these reactions are NAD+ or NADH. The 9-ketoreductases catalyze the reversible transformation of the functional group at C-9 and also the oxidation or reduction of the C-15 functional group. The preferred cofactors are NADP+ or NADPH. Bradykinin does not affect the activities of any of the three prostaglandin 9-ketoreductases. Flavin mononucleotide and the flavonoid, quercetin, as well as indomethacin, ethacrynic acid, and furosemide, inhibit all three 9-ketoreductases. An inhibitor of 9-ketoreductase isolated from chicken breast muscle also inhibits the three separable reductases, but the pattern of inhibition of the reductase that focuses at pH 5.7 differs from that of the reductases focusing at pH 7.8 and 8.2.