[Cytochrome P-450 in proteoliposomes: oligomeric structure of the LM2 isoform].
Crosslinking of protein molecules with bifunctional reagents and subsequent electrophoresis of the modified proteins revealed the presence of cytochrome P-450 LM 2 oligomers in proteoliposome membranes obtained in different ways and differing in their phospholipid composition. Data from a comparative analysis of cytochrome P-450 oligomeric structures in solution and in membrane are suggestive of the hexameric organization of cytochrome P-450 LM 2 within proteoliposome membranes.
Miasoedova
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Berndt
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D000818:Animals; D001436:Bacteriorhodopsins / Q000378:metabolism; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000378:metabolism*; D008081:Liposomes / Q000378:metabolism*; D008854:Microscopy, Electron; D008862:Microsomes, Liver / Q000201:enzymology; D011487:Protein Conformation; D011510:Proteolipids / Q000378:metabolism*; D011817:Rabbits
D003432:Cross-Linking Reagents; D007527:Isoenzymes; D008081:Liposomes; D011510:Proteolipids; C020485:proteoliposomes; D001436:Bacteriorhodopsins; D003577:Cytochrome P-450 Enzyme System
Tsitokhrom P-450 v proteoliposomakh: oligomernaia struktura izoformy LM2.