Covalent Structure of Collagen: Amino‐Acid Sequence of Chymotryptic Peptides from the Carboxyl‐Terminal Region of α2‐CB3 of Chick‐Skin Collagen

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Abstract
The amino acid sequence of chymotryptic peptides C4 and C5 which together make up 206 COOH-terminal residues of .alpha.2-CB3 of chick skin collagen is described. This in combination with the sequence of 132 residues from the amino-terminal region published earlier completes the total amino acid sequence of the large CNBr peptide, .alpha.2-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 .alpha.(I) chain showed striking variance of over 51% within the same species.