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Abstract Glycopeptides from carp swim bladder, guinea pig skin, and human skin collagens were prepared by sequential collagenase-trypsin digestion. Gel filtration on Sephadex G-25 permitted the isolation of a low molecular weight fraction containing most of the hydroxylysyl glycosides present in the parent collagen. Application of this fraction to a Dowex 50X-8 ion exchange column consistently resulted in distinctive glycopeptide patterns characteristic of each collagen. The glycohexapeptide, Gly-Met-Hyl (Gal-Glc)-Gly-His-Arg, which had been previously characterized in digests of soluble guinea pig skin collagen, was found in significant quantities in all three collagens examined, but the carp and human collagens each revealed an additional major glycopeptide. The subtractive Edman procedure was used in establishing amino acid sequences, and alkaline hydrolysis was used to confirm the composition and mode of attachment of the carbohydrate side chains. The predominant glycopeptide isolated from carp swim bladder collagen was Gly-Ile-Hyl(Gal-Glc)-Gly-His-Arg, while the structure of the unique glycopeptide isolated from human skin collagen was Gly-Phe-Hyl(Gal-Glc)-Gly-Ile-Arg. A possible role of the carbohydrate side chains in the organization of fibrils is discussed.
Morgan et al. (Thu,) studied this question.
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