20 beta-hydroxysteroid dehydrogenase of neonatal pig testis: purification and some properties.

@article{Nakajin198820BD,
  title={20 beta-hydroxysteroid dehydrogenase of neonatal pig testis: purification and some properties.},
  author={Shizuo Nakajin and Shuji Ohno and Masato Shinoda},
  journal={Journal of biochemistry},
  year={1988},
  volume={104 4},
  pages={565-9}
}
20 beta-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,20 beta… CONTINUE READING