Partial purification of prostaglandin E2-9-ketoreductase and prostaglandin-15-hydroxydehydrogenase from ovarian tissues of rabbits.
Prostaglandin E2-9-ketoreductase (PGE2-9-KR) and prostaglandin-15-hydroxydehydrogenase (PG-15-HDH) have been purified 25.0- and 15.4-fold, respectively. The rate equations of the enzyme reaction for two substrates were used for the determination of kinetic constants. The Michaelis constant, Km, for PGE2 was 122 microM for the PGE2-9-KR and 8 microM for the PG-15-HDH. The presence of both enzymes in ovarian tissues of rabbits indicate that these tissues may be able to synthesize and metabolize PGF2 alpha.
D000818:Animals; D015237:Dinoprost; D015232:Dinoprostone; D005260:Female; D006911:Hydroxyprostaglandin Dehydrogenases / Q000302:isolation & purification*; D007700:Kinetics; D010053:Ovary / Q000201:enzymology* / Q000502:physiology; D011458:Prostaglandins E / Q000378:metabolism; D011460:Prostaglandins F / Q000096:biosynthesis / Q000378:metabolism; D011817:Rabbits
D011458:Prostaglandins E; D011460:Prostaglandins F; D015237:Dinoprost; D006911:Hydroxyprostaglandin Dehydrogenases; C035859:15-hydroxyprostaglandin dehydrogenase; C035858:prostaglandin-E2 9-reductase; D015232:Dinoprostone