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.
Taniguchi
H
H
Institute of Experimental Pathology, German Cancer Research Center, Heidelberg, F.R.G.
Pyerin
W
W
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