Purification and characterization of 7 alpha-hydroxy-4-cholesten-3-one 12 alpha-hydroxylase.

@article{Ishida1992PurificationAC,
  title={Purification and characterization of 7 alpha-hydroxy-4-cholesten-3-one 12 alpha-hydroxylase.},
  author={Hajime Ishida and Mitsuhide Noshiro and Kyuichiro Okuda and Minor J. Coon},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 30},
  pages={21319-23}
}
The isoform of cytochrome P450 that catalyzes the 12 alpha-hydroxylation of 7 alpha-hydroxy-4-cholesten-3-one, an intermediate in the conversion of cholesterol to cholic acid, was purified to homogeneity from rabbit liver microsomes. The extent of purification in the various steps was judged by an assay involving high performance liquid chromatography. The purified enzyme showed a single band on SDS-polyacrylamide gel electrophoresis (M(r) = 50,000). The NH2-terminal amino acid sequence is as… CONTINUE READING