[Cytochrome b556 complexes solubilized from Micrococcus lysodeikticus membranes by triton X-100].
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.
D002499:Centrifugation, Density Gradient; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003580:Cytochromes / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008566:Membranes / Q000032:analysis / Q000648:ultrastructure; D008837:Micrococcus / Q000032:analysis* / Q000648:ultrastructure; D008854:Microscopy, Electron; D011092:Polyethylene Glycols; D012995:Solubility
D003580:Cytochromes; D011092:Polyethylene Glycols
Kompleksy tsitokhroma b556, soliubilizirovannye iz membran Micrococcus lysodeikticus tritonom X-100.