Purification of human placental prostaglandin 15-hydroxydehydrogenase

The NAD(+)-linked prostaglandin 15-hydroxydehydrogenase, which is responsible for the physiological inactivation of prostaglandins by catalysing the first step in the catabolism, was isolated and purified 995-fold from human placenta. The introduction of two new chromatographic steps in the purification procedure is responsible for an achieved specific activity of 1791 mU/mg. The molecular mass of the enzyme, as estimated by fast protein liquid chromatography, was 24,500 dalton. Sodium dodecyl sulphate discontinuous gel electrophoresis of the denatured enzyme revealed a molecular mass of 24,000 dalton. These data suggest that the enzyme consists of a single polypeptide chain.