20.BETA.-Hydroxysteroid dehydrogenase of neonatal pig testis. Localization in cytosol fraction and comparison with the enzyme from other species.

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Abstract
20.beta.-Hydroxysteroid dehydrogenase (20.beta.-HSD) was found in neonatal pig testes. The enzyme catalyzed the reduction of 17.alpha.-hydroxyprogesterone to 17.alpha.,20.beta.-dihydroxy-4-pregnen-3-one with oxidation of nicotinamide adenine dinucleotide phosphate, reduced form (NADPH). Identification of 17.alpha.,20.beta.-dihydroxy-4-pregnen-3-one as the product was achieved by thin layer chromatography, gas chromatography, high-erformance liquid chromatography, nuclear magnetic resonance spectroscopy and mass spectrometry. 20.beta.-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 20.beta.-HSD in comparison with that of mature pig testis. The 20.beta.-HSD activity was also found in the cytosol fraction of mouse, rat, dog and guinea pig testes, but the activities were very low.

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