20β-Hydroxysteroid Dehydrogenase of Neonatal Pig Testis : Localization in Cytosol Fraction and Comparison with the Enzyme from Other Species(Biological)

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20β-Hydroxysteroid dehydrogenase (2β-HSD) was found in neonatal pig testes. The enzyme catalyzed the reduction of 17α-hydroxyprogesterone to 17α,20β-dihydroxy-4-pregnen-3-one with oxidation of nicotinamide adenine dinucleotide phosphate, reduced form(NADPH). Identification of 17α,20β-dihydroxy-4-pregnen-3-one as the product was achieved by thin layer chromatography, gas chromatography, high-performance liquid chromatography, nuclear magnetic resonance spectroscopy and mass spectrometry. 20β-HSD activity was contained in the cytosol fraction of testis but not the microsomal or the mitochondrial fraction. Furthermore, the enzyme required the presence of NADPH or reduced nicotinamide adenine dinucleotide(NADH) as a cofactor, though NADH was far less effective than NADPH. The cytosol fraction of neonatal pig testis contained a large amount of 20β-HSD in comparison with that of mature pig testis. The 20β-HSD activity was also found in the cytosol fraction of mouse, rat, dog and guinea pig testes, but the activities were very low.
公益社団法人日本薬学会の論文
1987-06-25