Cytochrome b556 complexes solubilized from Micrococcus lysodeikticus membranes by triton X-100
Turgenbaeva, D.A.; Kharat'ian, E.F.; Zhukova, I.G.; Lukoianova, M.A.; Ostrovskii, D.N.
Biokhimiia 44(4): 729-737
ISSN/ISBN: 0320-9725 PMID: 435582 Accession: 039729474
The integral protein of cytochrome b556 after its solubilization with Triton X-100 from M. lysodeikticus 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. It is concluded that native protein complexes marked with cytochrome b556 are extracted from the membranes under their solubilization.