| FEBS Letters | |
| Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein | |
| Weber, Klaus1  Geisler, Norbert1  Plessmann, Uwe1  | |
| [1] Max Planck Institute for Biophysical Chemistry, D-3400 Goettingen, FRG | |
| 关键词: Keratin; Neurofilament; Desmin; GFA; Vimentin; | |
| DOI : 10.1016/0014-5793(83)81153-3 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020284832ZK.pdf | 374KB |
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