Steroids p. 477 - 496 (1987)
Update date:2022-08-29
Topics:
Chen
Nancarrow
Sweet
3β,20α-Hydroxysteroid oxidoreductase has been isolated from ovine fetal blood by a 2,370-fold purification scheme of ammonium sulfate fractionation, calcium phosphate gel adsorption, affinity chromatography, and fast performance liquid chromatography. A new high performance liquid chromatography-based assay for measuring 20α-reductase activity is described. The enzyme is a monomer with a molecular weight of 35,000 and uses NADPH as a cofactor for reductase activity. It reduces progesterone to 4-pregnan-20α-ol-3-one or 5α-dihydrotestosterone to 5α-androstan-3β,17β-diol with kinetic characteristics of Km = 30.8 μM and Vmax = 0.7 nmol min-1 (nmol of enzyme)-1 or Km = 74 μM and Vmax = 1.3 nmol min-1 (nmol of enzyme)-1, respectively. 5α-Dihydrotestosterone competitively inhibits 20α-reductase activity with a Ki value of 102 μM.
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