Cytochrome P450 1A2: oligomers in proteoliposomes.
The presence of oligomers of cytochrome P450 1A2 in membranes of proteoliposomes produced by the cholate-dialysis technique was demonstrated by cross-linking of protein molecules with bifunctional reagents followed by electrophoretic analysis of the modified proteins. A hexameric organization of cytochrome P450 1A2 in the membrane of proteoliposomes is suggested with high probability based on the comparison of the purified hemoprotein oligomeric structure in an aqueous medium and that in the proteoliposomes. The comparison was carried out using the same method.
Myasoedova
K N
KN
Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia. kinet@glas.apc.org.
D000818:Animals; D020355:Cholates; D003432:Cross-Linking Reagents; D019388:Cytochrome P-450 CYP1A2 / Q000737:chemistry* / Q000302:isolation & purification; D003956:Dialysis; D004591:Electrophoresis, Polyacrylamide Gel; D008081:Liposomes; D008099:Liver / Q000201:enzymology; D020836:Protein Structure, Quaternary; D011510:Proteolipids; D011817:Rabbits
D020355:Cholates; D003432:Cross-Linking Reagents; D008081:Liposomes; D011510:Proteolipids; C020485:proteoliposomes; D019388:Cytochrome P-450 CYP1A2