Partial purification and characterization of NADP-dependent 12alpha-hydroxysteroid dehydrogenase from Clostridium leptum.

@article{Harris1978PartialPA,
  title={Partial purification and characterization of NADP-dependent 12alpha-hydroxysteroid dehydrogenase from Clostridium leptum.},
  author={J. Harris and P. Hylemon},
  journal={Biochimica et biophysica acta},
  year={1978},
  volume={528 1},
  pages={
          148-57
        }
}
  • J. Harris, P. Hylemon
  • Published 1978
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • An NADP-linked 12α-hydroxysteroid dehydrogenase was purified 63-fold from crude extracts (105 000 × g supernatant fraction) of Clostridium leptum using Bio-Gel A-1.5 M and DEAE-cellulose column chromatography. The 63-fold purified enzyme preparation (specific activity 3.3 I.U./mg protein) had a pH optimum of 8.5–9.0. A molecular weight of approx. 225 000 was estimated for the catalytically active enzyme by molecular sieve chromatography. The enzyme converted both unconjugated bile acids as well… CONTINUE READING
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