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September 1, 1966Journal of Biological Chemistry299 citationsOpen Access

Evidence for the Linkage of a Disaccharide to Hydroxylysine in Tropocollagen

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WBWilliam T. ButlerLCLeon W. Cunningham

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Abstract

Abstract Soluble collagen from guinea pig skin has been subjected to sequential digestion with purified collagenase and trypsin. The small quantity of hexose present in the collagen can be detected in the digest largely as relatively basic glycopeptides. One of these glycopeptides has been obtained in pure form and accounts for at least 30% of the hexose of the original collagen. This glycopeptide has been shown to consist of a disaccharide of glucose and galactose linked O-glycosidically to the hydroxyl group of a hydroxylysine residue in a special peptide region of the collagen molecule. The amino acid composition and probable sequence in this region was shown to be -Gly-Met-Hyl(Glc, Gal)-Gly-His-Arg- A possible role for this structure in the formation of cross-links during collagen maturation is described.

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Butler et al. (1966) studied this question.

synapsesocial.com/papers/6a0c7d01d48675e494238017https://doi.org/10.1016/s0021-9258(18)99789-9
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The Site of Attachment of Hexose in Tropocollagen1965 · 40 citations
  2. 2Studies on mucoproteins VII. The linkage of the prosthetic group to aspartic and glutamic acid residues in bovine submaxillary gland mucoprotein1961 · 66 citations
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  4. 4PHOTOMETRIC NINHYDRIN METHOD FOR USE IN THE CHROMATOGRAPHY OF AMINO ACIDS1948 · 3,046 citations
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