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J. Biochem, 1988, Vol. 104, No. 4 565-569
© 1988 Japanese Biochemical Society

research-article

20ß-Hydroxysteroid Dehydrogenase of Neonatal Pig Testis: Purification and Some Properties1

Shizuo Nakajin2, Shuji Ohno and Masato Shinoda

Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hoshi University Shinagawa-ku, Tokyo 142

2To whom correspondence should be addressed

20ß-Hydroxysteroid dehydrogenase was purified from a cytosol fraction of neonatal pig testes to homogeneity as demonstrated by polyacrylamide gel electrophoresis (PAGE) and by isoelectric focusing. The molecular weight was estimated to be 30,500 using PAGE with sodium dodecyl sulfate and the gel filtration method. Molecular estimations showed that the purified enzyme consisted of a single polypeptide chain. It catalyzed the reduction of 17{alpha}-hydroxyprogesterone to 17{alpha} 20ß-dihydroxypregn-4-en-3-one with NADPH. Furthermore, the C21-steroids, such as progesterone, pregnenolone, 17{alpha}-hydroxypregnenolone, deoxycorticosterone, and deoxycortisol were also reduced by the purified enzyme. Apparent Km values for 17{alpha}-hydroxyprogesterone, progesterone, pregnenolone, and deoxycorticosterone were 9.4, 1.5, 4.0, and 8.6 µM, respectively. The enzyme did not show 20{alpha}-hydroxysteroid dehydrogenase activity. The maximum rate of enzyme activity was observed at 45°C and optimum pH was at pH 5.5. The enzyme activity was strongly inhibited by heavy metal ions such as Hg2+ and Cu2+.

1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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