Covalent structure of collagen: amino-acid sequence of chymotryptic peptides from the carboxyl-terminal region of alpha2-CB3 of chick-skin collagen.

The amino acid sequence of chymotryptic peptides C4 and C5 which together make up 206 COOH-terminal residues of alpha2-CB3 of chick skin collagen is described. This in combination with the sequence of 132 residues from the amino-terminal region published earlier [Dixit, Seyer, and Kang (1977) Eur. J. Biochem. 73, 213-221] completes the total amino acid sequence of the large CNBr peptide, alpha2-CB3 of chick skin collagen. The amino acid sequence was determined by automated Edman degradation of intact peptides C4 and C5 and their respective tryptic and maleylated tryptic peptides, and thermolytic peptides of C4. The comparison of the sequence with the homologous segment of alpha1(I) chain showed striking variance of over 51% within the same species.