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Intermediate Filaments from Bovine, Rat, and Human CNS: Mapping Analysis of the Major Proteins
Author(s) -
Chiu FungChow,
Korey Barry,
Norton William T.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb09954.x
Subject(s) - protein filament , cyanogen bromide , molecular mass , protein subunit , intermediate filament , proteolysis , biology , gel electrophoresis , cleavage (geology) , neurofilament , biochemistry , chemistry , peptide sequence , cytoskeleton , cell , enzyme , immunology , paleontology , immunohistochemistry , fracture (geology) , gene
Intermediate filaments were isolated by an axon‐flotation method from bovine, rat, and human CNS. Gel electrophoresis showed four major proteins, having molecular weights of about 50,000, 70,000, 160,000, and 210,000, to be present in filaments of all three species. Small differences in molecular weights and major differences in relative distribution of the filament proteins were observed among species. In bovine and rat brain the predominant protein was the 50,000 band, but in human brain the 70,000 band was present in greatest amount. Each filament protein of the three species was studied by peptide mapping using limited proteolysis and cyanogen bromide cleavage. Within the same molecular weight group, filament proteins from different species gave similar maps with both techniques. Some degree of heterogeneity was also observed. However, filament proteins of different molecular weights of the same species gave distinctly different maps. These studies rule out the possibility that filament proteins from different molecular weight groups are related to each other by oligomerization; nor is it likely that the lower molecular weight proteins are derived from the subunit of molecular weight 210,000.