Cross-Linking study of cytochrome P450 1A2 in proteoliposomes.
Proteoliposomes, containing cytochrome P450 1A2, were obtained by the cholate-dialysis technique. The effect of bifunctional cross-linking reagents on the purified hexameric cytochrome P450 1A2 in an aqueous medium and on the proteoliposomal P450 1A2 have been compared. Electrophoretic analysis of the modified proteins demonstrated the same oligomeric (hexameric) organization of the hemoprotein in each case.
Myasoedova
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N. N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow.
Magretova
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D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry*; D019388:Cytochrome P-450 CYP1A2 / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D022781:Hepatocytes / Q000378:metabolism*; D007425:Intracellular Membranes / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry; D011510:Proteolipids / Q000737:chemistry*; D011817:Rabbits; D020358:Sodium Cholate / Q000737:chemistry
D003432:Cross-Linking Reagents; D010743:Phospholipids; D011510:Proteolipids; C020485:proteoliposomes; D019388:Cytochrome P-450 CYP1A2; D020358:Sodium Cholate