Prostaglandin E2 9-keto reductase from bovine term placenta.

The aim of the following study was to determine the activity and physico-chemical properties of prostaglandin E2 9-keto reductase from bovine placenta. Placental tissues obtained immediately after parturition were subjected to purification procedure consisting of homogenization, affinity chromatography, gel filtration and allowed to electrophoresis. The activity of enzyme was measured spectrophotometrically. The purification procedures receive 135-fold purified enzyme preparate of the molecular weight of 45 kDa with the following kinetic values: Michaelis constant for PGE2, 117 microM and max velocity 183 pmol/min. The activity of enzyme was also detected with 20 alpha-hydroxypregn-4en-3-one and with 9,10-phenanthrenquinone (Michaelis constant 22 microM and 6 microM, respectively). The determination of physico-chemical properties of prostaglandin E2 9-keto reductase, performed for the first time in bovine placenta, should aid the understanding of the metabolism of prostaglandins and their biological importance in physiological and pathological conditions in cattle.