Partial isolation and characterization of the 15-hydroxyprostaglandin dehydrogenases and 9-ketoprostaglandin reductases in rabbit kidney.

Three types of 15-hydroxyprostaglandin dehydrogenase were identified in rabbit whole kidney homogenate when the centrifuged homogenate was sequentially fractionated by ammonium sulfate precipitation, DEAE-cellulose and Matrex Gel Blue A chromatographies, and Sephadex gel filtration. The first type is not adsorbed to DEAE-cellulose (peak 1). It catalyzes oxidoreduction of prostaglandins at both the C-15 and C-9 positions, is more active with NADP than NAD, is inhibited by indomethacin and ethacrynic acid, and migrates as three bands on disc gel electrophoresis. The second type is adsorbed to DEAE-cellulose (peak 2). It also migrates as multiple electrophoretic bands, has similar catalytic actions and co-factor requirements as the peak 1 enzyme and is inhibited by indomethacin and ethacrynic acid. A third type of 15-hydroxyprostaglandin dehydrogenase is also adsorbed to DEAE-cellulose but is partially separable from the other peak 2 enzymes on Matrex Gel Blue A and differs from those enzymes in preferentially oxidizing PGI2. It migrates as a single electrophoretic band and is also inhibited by indomethacin and ethacrynic acid.