The amino acid sequence of chick skin collagen alpha1-CB6A, a peptide containing 107 residues obtained from the helical region near the carboxy-terminus of the alpha1(I) chain by cyanogen bromide cleavage, has been determined. This was accomplished by automated Edman degradation of the hydroxylamine-produced fragments and of the tryptic peptides prepared with and without prior maleylation. The data show that this portion of the alpha1(I) chain from chick skin is identical in 90 percent of the residues to the corresponding peptide region of calf skin collagen reported previously.

No abstract