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Incorporation of the cytochrome P-450 monooxygenase system into large unilamellar liposomes using octylglucoside,especially for measurements of protein diffusion in membranes |
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| Authors: | D Schwarz K Gast HW Meyer U Lachmann MJ Coon K Ruckpaul |
| Institution: | 1. Dept. Biocatalysis, Central Institut for Molecular Biology, Academy of Sciences of GDR, 1115 Berlin, GDR;2. Dept. Molecular Biophysics, Central Institut for Molecular Biology, Academy of Sciences of GDR, 1115 Berlin, GDR;3. Lab. Electron Microscopy., Dept. Medicine, Friedrich Schiller University, Jena, GDR;4. Central Institute for Isotopic and Radiation Research, Academy of Sciences of GDR, 1115 Berlin, GDR;5. Dept. Biological Chemistry, The University of Michigan, Ann Arbor, Michigan USA |
| Abstract: | 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 octylglucoside 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. |
| Keywords: | P-450 LM2 cytochrome P-450 isozyme induced in rabbit liver by phenobarbital (EC 1 14 14 1 ) reductase NADPH cytochrome P-450 reductase (EC 1 6 4 2 ) PC phosphatidylcholine PE phosphatidylethanolamine PA phosphatidic acid octylglucoside n-octyl-β-D-glucopyranoside ML microsomal lipid extract |
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