Homologous regions of collagen α1(I) and α1(II) chains: Apparent clustering of variable and invariant amino acid residues

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Summary

The amino acid sequence of 75 residues from the central portion of the α1(II) chain of bovine cartilage collagen is reported and compared to that of a homologous region of the α1(I) chain of bovine skin collagen. The comparison suggests that collagen α chains contain regions with a high level of sequence variability alternating with other regions displaying few, or no, interchain sequence differences. The presence of two residues of galactosylhydroxylysine in the α1(II) sequence, absent in α1(I), suggest reasons for the relatively high carbohydrate content of α1(II).

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