title: [Bacterial membrane proteins. Properties of Micrococcus lysodeikticus NADH dehydrogenase].
abstract: NADH dehydrogenase was isolated from M. lysodeikticus membranes with FAD as a prosthetic group. It was found the enzyme molecular weight is about 140000 in 0,01 M phosphate buffer, pH 7,4 in 1% Triton X-100. The enzyme molecules are dimers consisting of two subunits with molecular weight of 70000. The content of alpha-helical regions is 30%, that of beta-forms is 13%. The protein globule is cross-linked with the disulfide bonds and has hydrophobic regions on its surface.
mesh_terms: D002462:Cell Membrane / Q000201:enzymology; D004220:Disulfides; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000302:isolation & purification; D008837:Micrococcus / Q000201:enzymology*; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification; D011485:Protein Binding; D011487:Protein Conformation; D013499:Surface Properties
chemical_list: D004220:Disulfides; D046911:Macromolecular Substances; D008565:Membrane Proteins; D009247:NADH, NADPH Oxidoreductases
vernacular_title: Belki bakterial'nykh membran. Svoĭstva NADH-degidrogenazy iz Micrococcus lysodeikticus.