Apoprotein formation and heme reconstitution of cytochrome P-450cam.

@article{Wagner1981ApoproteinFA,
  title={Apoprotein formation and heme reconstitution of cytochrome P-450cam.},
  author={George W. Wagner and M Suarez - Perez and William A. Toscano and Irwin Clyde Gunsalus},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 12},
  pages={6262-5}
}
Apoprotein suitable for heme reconstitution has been prepared by an acid/butanone extraction of cytochrome P-450cam at pH 2.5. Absorption spectra of apo-P-450cam indicate less than 2% residual holoenzyme. Four tryptophan residues per molecule were estimated from the aromatic absorbance region of denatured apoprotein. Heme-reconstituted holoprotein was purified in 30% yield to a specific activity equivalent to the native enzyme. Absorption and EPR spectra of 57Fe- and 54Fe-heme-enriched P-450cam… CONTINUE READING