The covalent structure of collagen. Amino acid sequence of α1 CB5 glycopeptide and α1 CB4 from chick skin collagen

Andrew Kang, S. N. Dixit, C. Corbett, J. Gross

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The amino acid sequences of chick skin α1 CB4 and α1 CB5 have been determined by automated Edman degradation of the intact peptides and of their tryptic and chymotryptic peptides. The two peptides contain 47 and 37 residues and comprise residues 56 to 102 and 103 to 139, respectively, of the α1(I) chain. In addition, α1 CB5 is the major hexose containing peptide, previously reported to be active in mediating platelet aggregation. A comparison of the sequence with previously reported data on the homologous region of the rat skin α1(I) chain indicates that there are only three interspecies differences, or a sequence identity of 96%.

Original languageEnglish (US)
Pages (from-to)7428-7434
Number of pages7
JournalJournal of Biological Chemistry
Volume250
Issue number18
StatePublished - Dec 1 1975

Fingerprint

Glycopeptides
Amino Acid Sequence
Skin
Collagen
Amino Acids
Peptides
Hexoses
Platelets
Platelet Aggregation
Rats
Agglomeration
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The covalent structure of collagen. Amino acid sequence of α1 CB5 glycopeptide and α1 CB4 from chick skin collagen. / Kang, Andrew; Dixit, S. N.; Corbett, C.; Gross, J.

In: Journal of Biological Chemistry, Vol. 250, No. 18, 01.12.1975, p. 7428-7434.

Research output: Contribution to journalArticle

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