Literature DB >> 1165248

The covalent structure of collagen. Amino acid sequence of alpha1-CB5 glycopeptide and alpha1-CB4 from chick skin collagen.

A H Kang, S N Dixit, C Corbett, J Gross.   

Abstract

The amino acid sequences of chick skin alpha1-CB4 and alpha1-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 alpha1(I) chain. In addition, alpha1-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 alpha1(I) chain indicates that there are only three interspecies differences, or a sequence identity of 96%.

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Year:  1975        PMID: 1165248

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Visualization of Genetic Drift Processes Using the Conserved Collagen 1α1 GXY Domain.

Authors:  Anne J Kleinnijenhuis
Journal:  J Mol Evol       Date:  2019-03-13       Impact factor: 2.395

2.  Domain-Specific Proteogenomic Analysis of Collagens to Evaluate De Novo Sequencing Results and Database Information.

Authors:  Anne J Kleinnijenhuis; Frédérique L van Holthoon
Journal:  J Mol Evol       Date:  2018-05-02       Impact factor: 2.395

3.  Isolation and hydroxylysine glycoside content of some cyanogen bromide-cleaved fragments of collagen from bovine corneal stroma.

Authors:  N A Panjwani; J J Harding
Journal:  Biochem J       Date:  1978-06-01       Impact factor: 3.857

4.  Chymotryptic and tryptic peptides of fragment alpha 1-CB3 from bovine corneal collagen. Pinpointing the sites of hexose attachment.

Authors:  N A Panjwani; J J Harding
Journal:  Biochem J       Date:  1978-06-01       Impact factor: 3.857

  4 in total

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