Expression in Escherichia coli of functional cytochrome P450c17 lacking its hydrophobic amino-terminal signal anchor.

@article{Sagara1993ExpressionIE,
  title={Expression in Escherichia coli of functional cytochrome P450c17 lacking its hydrophobic amino-terminal signal anchor.},
  author={Yasuaki Sagara and Henry J. Barnes and Michael R. Waterman},
  journal={Archives of biochemistry and biophysics},
  year={1993},
  volume={304 1},
  pages={272-8}
}
A truncated form of bovine microsomal 17 alpha-hydroxylase cytochrome P450 (P450c17) lacking its amino-terminal hydrophobic signal anchor sequence (delta 2-17) was expressed in Escherichia coli to give more than 600 nmol P450 per liter using XL1-blue as the host. The expression level of the truncated P450c17 showed variation among different host strains. When intact E. coli cells were used for analysis, the truncated P450c17 showed the typical cytochrome P450 CO-difference spectrum and type I… CONTINUE READING