Expression of cytochrome P450 2D6 in Escherichia coli, purification, and spectral and catalytic characterization.

@article{Gillam1995ExpressionOC,
  title={Expression of cytochrome P450 2D6 in Escherichia coli, purification, and spectral and catalytic characterization.},
  author={Elizabeth M J Gillam and Zhi Hua Guo and M. Virginia Mart{\'i}n and Christopher M. Jenkins and F Peter Guengerich},
  journal={Archives of biochemistry and biophysics},
  year={1995},
  volume={319 2},
  pages={540-50}
}
Cytochrome P450 (P450) 2D6 is the classic human liver debrisoquine 4-hydroxylase, the first human P450 for which genetic polymorphism was clearly demonstrated. We prepared 11 different constructs of P450 2D6, with modification at the N-terminus, for expression in Escherichia coli with the vector pCW. These varied considerably in levels of expression of apo- and holoprotein, with the best yield being obtained in a system in which much of the N-terminal hydrophobic segment was removed. Production… CONTINUE READING