Characterization of a major form of rat hepatic microsomal cytochrome P-450 induced by isoniazid.

@article{Ryan1985CharacterizationOA,
  title={Characterization of a major form of rat hepatic microsomal cytochrome P-450 induced by isoniazid.},
  author={Dene E. Ryan and Lata Ramanathan and S. Iida and Paul E. Thomas and Mitsuru Haniu and John E. Shively and Charles S. Lieber and Wayne Levin},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 10},
  pages={
          6385-93
        }
}
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309 Citations
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Quantitative high-pressure liquid chromatographic assays were developed that separate progesterone and 17 authentic monohydroxylated derivatives and indicated that P-450k or an immunochemically related isozyme contributed greater than 80% of the 21-hydroxylase activity observed in microsomes from phenobarbital-induced rats.
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Regioselective progesterone hydroxylation catalyzed by eleven rat hepatic cytochrome P-450 isozymes.

Quantitative high-pressure liquid chromatographic assays were developed that separate progesterone and 17 authentic monohydroxylated derivatives and indicated that P-450k or an immunochemically related isozyme contributed greater than 80% of the 21-hydroxylase activity observed in microsomes from phenobarbital-induced rats.

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