[New data on the molecular heterogeneity of brain-specific protein S100].
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.
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D000818:Animals; D001923:Brain Chemistry; D002850:Chromatography, Gel; D008970:Molecular Weight; D051381:Rats; D009418:S100 Proteins / Q000032:analysis*
D009418:S100 Proteins
Novye dannye o molekuliarnoĭ geterogennosti mozgospetsificheskikh belkov gruppy S100.