Section 6
Chapter 5,085

Cytochrome b 556 complexes solubilized with triton x 100 from micrococcus lysodeikticus membranes

Turgenbaeva, D.A.; Kharat'yan E.F.; Zhukova, I.G.; Lukoyanova, M.A.; Ostrovskii, D.N.

Biokhimiya 44(4): 729-737


Accession: 005084585

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The integral protein of cytochrome b566 after its solubilization with Triton X-100 from M. lysodeikticus [luteus] membranes was studied. The cytochrome was found in complexes differing in charge and size during preparative gel electrophoresis and centrifugation in a sucrose concentration gradient. Cytochrome b556, being in complexes, retains its ability to be reduced by NADH dehydrogenase. The electron micrographs of the membranes after solubilization by Triton X-100 demonstrated the maintenance of the membrane structure. Native protein complexes marked with cytochrome b556 are extracted from the membranes under their solubilization.

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