Purification of Cytochromes P450: Products of Bacterial Recombinant Expression Systems

Abstract

A general procedure for the solubilization of cytochrome P450 (P450) from bacterial membranes specifically for a human P450 expressed heterologously in the host Escherichia coli is described. The example involves the use of a P450 (3A4) with a C-terminal oligohistidine tag and includes sequential DEAE and metal affinity chromatography.