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. 1987 Jun 1;244(2):303–309. doi: 10.1042/bj2440303

Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen.

K Barnard 1, N D Light 1, T J Sims 1, A J Bailey 1
PMCID: PMC1147991  PMID: 3117039

Abstract

The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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