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.