| Literature DB >> 3743769 |
V L Tsuprun, K N Myasoedova, P Berndt, O N Sograf, E V Orlova, A I Archakov, V P Skulachev.
Abstract
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.Entities:
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Year: 1986 PMID： 3743769 DOI： 10.1016/0014-5793(86)80861-4
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124