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
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.