Incorporation of the cytochrome P-450 monooxygenase system into large unilamellar liposomes using octylglucoside, especially for measurements of protein diffusion in membranes.
Cytochrome P-450 and NADPH cytochrome P-450 reductase were incorporated into large unilamellar lipid vesicles (200-300 nm in diameter) removing octylglucoside from mixed micelles by dialysis. The large size of the protein-containing liposomes guarantees a negligibly small vesicle tumbling. Such large vesicles are better suited for studies of protein rotation in reconstituted membranes than vesicles prepared by use of bile salts. At present the octyl-glucoside reconstituted monooxygenase system seems to be the most appropriate model for studying protein-protein and protein-lipid interactions in liver microsomes due to the similarity with respect to the main structural and functional properties, including size.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System; D003902:Detergents; D005614:Freeze Fracturing; D005960:Glucosides / Q000494:pharmacology*; D006027:Glycosides / Q000494:pharmacology*; D066298:In Vitro Techniques; D008081:Liposomes / Q000378:metabolism*; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism*; D008862:Microsomes, Liver / Q000201:enzymology / Q000378:metabolism; D010105:Oxygenases / Q000378:metabolism*; D011817:Rabbits
D003902:Detergents; D005960:Glucosides; D006027:Glycosides; D008081:Liposomes; D008565:Membrane Proteins; C018619:octyl-beta-D-glucoside; D003577:Cytochrome P-450 Enzyme System; D010105:Oxygenases