Separation and purification of component proteins of the cytochrome P-450-dependent microsomal monooxygenase system by high-performance liquid chromatography.

The component proteins of the hepatic microsomal monooxygenase system, including various cytochrome P-450 isozymes, were separated and isolated from liver microsomes of untreated rabbits by Aminohexyl Sepharose and high-performance liquid chromatography (TSK preparative DEAE 5-PW, Bio-Rad HPHT). In addition to the known cytochrome P-450 isozymes, two new isozymes and one variant of the major isozyme were isolated. The monooxygenase activity was reconstituted by incorporating the purified proteins into liposomal membranes.