Abstract

Insoluble guinea-pig skin collagen and insoluble dermal scar collagen were cleaved with CNBr and the peptides derived from the α 1- chain were separated by ion-exchange and molecular-sieve chromatography. Comparison of the peptides from scar collagen with those from skin collagen showed that the former contained more hydroxylysine. Separation of the CNBr peptides showed that this increase in hydroxylysine was found not only in the non-helical regions, but was also seen down the helical portion of the molecule. Separation of the peptides revealed the presence of more peptides in digests of skin collagen than those of scar, and these have been attributed to the presence of Type III collagen in skin, but no evidence was found for the presence of this Type III collagen in dermal scar tissue.

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