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- W2024294385 abstract "Abstract The 105g supernatant of rat ovarian homogenates is shown to contain an NAD-dependent 3β-hydroxysteroid oxidoreductase (3β-HSOR) and an NADP-dependent 3α-hydroxysteroid oxidoreductase (3α-HSOR), which catalyze the conversion of 3-oxo-5α-androstanes and 3-oxo-5α-pregnanes to the corresponding 3α- and 3β-hydroxysteroids. Both enzymes act reversibly. The products were identified by gas-chromatography, and enzyme kinetics were studied by continuous spectrophotometric determination of the reduced pyridine nucleotides. The enzymes were present throughout the oestrous cycle; the activity of 3β-HSOR was higher on the day of pro-oestrus than at other stages of the cycle. Unlike 20α-hydroxysteroid dehydrogenase, 3α-HSOR is present in the ovaries of prepubertal rats. 3β-HSOR differs from 5-en-3β-hydroxysteroid dehydrogenase in substrate specificity. 3β-HSOR was found exclusively in the cytosol fraction precipitated at 2 M ammonium sulphate, whereas 80% of the 3α-HSOR activity was recovered in the fraction precipitated at 4M. 3α-HSOR was further purified to five times its original specific activity by gel filtration on Sephadex G-100. It is eluted with a fraction of mol. wt. 20,000–40,000 Daltons and is electrophoretically distinct from 20α-hydroxysteroid dehydrogenase." @default.
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- W2024294385 date "1975-08-01" @default.
- W2024294385 modified "2023-09-25" @default.
- W2024294385 title "Separation and characterization of two 3-hydroxysteroid oxidoreductases from the soluble fraction of rat ovarian cells" @default.
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- W2024294385 doi "https://doi.org/10.1016/0022-4731(75)90106-5" @default.
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