Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen alpha 1(I) chain
The primary structure of chick skin collagen alpha 1-CB8, the 279-residue CNBr peptide from the helical portion of the alpha 1(I) chain, has been determined by automated amino acid sequence analysis of tryptic peptides of the maleylated and of the cyclohexanedione-treated material, of thermolytic pe...
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Veröffentlicht in: | Biochemistry (Easton) 1982-04, Vol.21 (9), p.2048-2055 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The primary structure of chick skin collagen alpha 1-CB8, the 279-residue CNBr peptide from the helical portion of the alpha 1(I) chain, has been determined by automated amino acid sequence analysis of tryptic peptides of the maleylated and of the cyclohexanedione-treated material, of thermolytic peptides, and of a single 40-residue chymotryptic fragment. The sequence thus obtained showed 95% identity with that of the corresponding peptide from rat collagen. Completion of this work permits the assembly of the complete helical amino acid sequence of the chick skin alpha 1(I) chain. |
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ISSN: | 0006-2960 |
DOI: | 10.1021/bi00538a011 |