Abstract
The entire sequence of α2‐CB2 from calf skin collagen, a cyanogen‐bromide‐derived peptide from the central portion of the α2 chain containing 30 amino‐acid residues was established. The sequence of 22 N‐terminal residues of α2‐CB2 from human and rabbit skin collagen and of 26 residues of the corresponding peptide from pig skin collagen were also determined. Comparison of the sequences revealed six definite positions within the first 21 amino‐acid residues of the peptide in which substitutions occurred, suggesting a portion of high sequence variability within the α2 chain.
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