title: [New data on the molecular heterogeneity of brain-specific protein S100].
abstract: A comparative study of distribution of labeled products of endogenous limited proteolysis of the "major" (MF) and "minor" (S100-26) fractions of proteins S100 from rat brain by ion-exchange chromatography was carried out with a view of testing the hypothesis on the formation of proteins S100 molecular associates as a possible cause of molecular weight heterogeneity of proteins S100. There is evidence that proteins S100-MF and S100-26 are different species of brain-specific S100 proteins. The experimental results also suggest that the brain-specific proteins S100-MF and S100-26 are adsorbed both by glial cells and by neurons. Some physico-chemical properties of peptide proteolytic products of various species of proteins S100 were investigated.
authors: M A
authors: MA
authors: Gruden'
authors: A B
authors: AB
authors: Poletaev
mesh_terms: D000818:Animals; D001923:Brain Chemistry; D002850:Chromatography, Gel; D008970:Molecular Weight; D051381:Rats; D009418:S100 Proteins / Q000032:analysis*
chemical_list: D009418:S100 Proteins
vernacular_title: Novye dannye o molekuliarnoĭ geterogennosti mozgospetsificheskikh belkov gruppy S100.