Quaternary structure of the liver microsomal cytochrome P-450.
Cytochrome P-450LM2 was isolated from rabbit liver microsomes in a form which was shown to be homogeneous in AcA-22 Ultrogel and ultracentrifugation studies. The molecular mass determined by sedimentation equilibrium roughly corresponded to hexamer composed of 56 kDa monomers. Hexamer structure of the cytochrome was directly demonstrated by electron microscopic study. In the cytochrome P-450LM2 hexamer, monomers seem to be arranged in two layers (three monomers in the layer) in such a way that each monomer occupies a position at the vertices of a triangular antiprism with a 32 point group symmetry.
D000818:Animals; D003201:Computers; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008297:Male; D008854:Microscopy, Electron; D008862:Microsomes, Liver / Q000201:enzymology*; D011817:Rabbits; D014461:Ultracentrifugation
D046911:Macromolecular Substances; D003577:Cytochrome P-450 Enzyme System