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Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein
Author(s) -
Geisler Norbert,
Plessmann Uwe,
Weber Klaus
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81153-3
Subject(s) - vimentin , peptide sequence , intermediate filament , chemistry , amino acid , intermediate filament protein , sequence (biology) , protein filament , biochemistry , microbiology and biotechnology , biology , cytoskeleton , cell , immunohistochemistry , gene , immunology
The amino‐terminal 98 residues of porcine vimentin have been determined by amino acid sequence studies. Extensive overlap is seen with the corresponding region of the carboxyterminal 448 residues of hamster vimentin predicted from DNA sequence studies, which left the very amino‐terminal region unknown. The combined data show that contrary to gel electrophoretic results, mammalian vimentin contains only about 467 residues, and that species‐specific drift occurs mainly in the amino‐terminal non‐α‐helical array. The results are discussed parallel to emerging concepts on intermediate filament protein diversity.