Abstract
Abstract Treatment of human placenta microsomes with phospholipase A or D inhibits the 17β-hydroxysteroid dehydrogenase [17β-HSD] activity, parallel with the hydrolysis of membrane phospholipids. The 17β-HSD activity of phospholipase treated microsomes is reactivated by synthetic phospholipids. The distribution of 17β-HSD activity in subfractions of original microsomes and of phospholipase treated microsomes obtained by zonal centrifugation was studied. Solubilization of the microsomal 17β-HSD was achieved by phospholipase A treatment. Two 17β-HSD were solubilized from human placenta microsomes by phospholipase A treatment and were further purified by ammonium sulphate precipitation, gel filtration on BioGel A-0.5 m, DEAESephadex chromatography and by isoelectric focusing. The enzymes were purified 25.8 and 17.4 times. The isoelectric points and molecular weights of the two 17β-HSD were determined. Both enzymes are of a 17β-HSD type. One of the 17β-HSD, however, was sensitive to estradiol- 17β, the other to testosterone. The question of whether the two enzymes constitute a monomer and a dimer of the same 17β-HSD or are completely different enzymes, is discussed.
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