The amino acid sequence of 120 residues in the N-terminal region of the alpha1-chain of calf skin collagen (comprising the cyanogen-bromide-derived peptides alpha1-CB2, alpha1-CB4 and alpha1-CB5) has been determined by automated Edman degradation. The lysyl residue in position 87 is completely hydroxylated, while those in positions 99 and 108 partially hydroxylated. Two substitutions are found with respect to the homologous region of the alpha1-chain from rat skin collagen. Positions 101 and 102 of calf skin collagen are occupied by Asp-Ala, in rat skin collagen by Asn-Thr. The extensive homology in this region is remarkable and is not found in other regions of the alpha1 and alpha2-chain.
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Fietzek et al. (1975) studied this question.
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