Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes.

@article{French1979PropertiesON,
  title={Properties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes.},
  author={John S. French and Minor J. Coon},
  journal={Archives of biochemistry and biophysics},
  year={1979},
  volume={195 2},
  pages={
          565-77
        }
}
Abstract NADPH-cytochrome P -450 reductase has been purified to electrophoretic homogeneity from rabbit liver microsomes by a procedure that may be used in conjunction with the isolation of the major forms of cytochrome P -450. The purified reductase is active in a reconstituted hydroxylation system containing P -450LM 2 or P -450LM 4 . The enzyme contains one molecule each of FMN and FAD per polypeptide chain having an apparent minimal molecular weight of 74,000. Immunological techniques… CONTINUE READING

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Beta sheet 2-alpha helix C loop of cytochrome P450 reductase serves as a docking site for redox partners.

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