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pubmed:abstractText |
The amino acid sequence of alpha1-CB3, a peptide containing 149 residues obtained from the central portion of the alpha1(I) chain of chick skin collagen by cyanogen bromide cleavage, has been determined. As in the other sequences from the helical region of collagen chains, the repeating triplet Gly-X-Y extends throughout the length of the peptide. These data allow a comparison of the sequence to that of alpha1-CB3 from calf and rat skin collagens. As compared with calf, the chick peptide contains 14 amino acid differences, whereas it contains 17 residue differences from the rat peptide. Thus, the sequence identity level is 91 and 89 percent, respectively, in comparison to the calf and rat peptides. These values are significantly greater than the value of 97 percent observed between the peptide of the two mammalian species and reflect the greater phylogenetic distance of the species compared.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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