Cytochrome P-450: hexameric structure of the purified LM4 form.
Purified cytochrome P-450LM4 was found to be monodisperse in 20% glycerol by analytical ultracentrifugation. Its S20,w value was quite similar to that of hexameric P-450LM2. At lower glycerol concentrations the P-450LM4 showed a tendency to aggregate. The P-450LM4 oligomers were immobilized on Ultrogel A4 under conditions allowing only one covalent link to the matrix per oligomer. In the presence of SDS, the oligomers dissociated leaving only 1/6th of the initial amount of bound protein on the matrix, suggesting that the purified P-450LM4 is a hexamer. This was confirmed by electron microscopy. The quaternary structure of the P-450LM4 was similar to that demonstrated earlier for P-450LM2.
Myasoedova
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N.N. Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow.
Tsuprun
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D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D008854:Microscopy, Electron; D011487:Protein Conformation; D011817:Rabbits; D014461:Ultracentrifugation
D003577:Cytochrome P-450 Enzyme System