Mechanism-based inactivation of cytochrome P450 2B1 by 9-ethynylphenanthrene.

@article{Roberts1995MechanismbasedIO,
  title={Mechanism-based inactivation of cytochrome P450 2B1 by 9-ethynylphenanthrene.},
  author={Elizabeth S. Roberts and Nancy Eddy Hopkins and E J Zaluzec and Douglas A. Gage and William L. Alworth and Paul F. Hollenberg},
  journal={Archives of biochemistry and biophysics},
  year={1995},
  volume={323 2},
  pages={295-302}
}
The 7-ethoxycoumarin O-deethylase activity of rat cytochrome P450 (P450) 2B1 was inactivated by 9-ethynylphenanthrene (9EPh) in a time- and NADPH-dependent manner, and the loss of activity followed pseudo-first-order kinetics. At 20 degrees C, the extrapolated maximal rate constant of inactivation (kinactivation) was 0.45 min-1 and the inactivator concentration required for half-maximal inactivation (KI) was 138 nM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and HPLC… CONTINUE READING

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