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.
Institute of Experimental Pathology, German Cancer Research Center, Heidelberg, F.R.G.
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Taniguchi
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Pyerin
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000302:isolation & purification*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000302:isolation & purification*; D010449:Peptide Mapping; D011506:Proteins / Q000302:isolation & purification*; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
D007527:Isoenzymes; D011506:Proteins; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases