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. 1980 Feb 1;185(2):373–381. doi: 10.1042/bj1850373

The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids.

N D Light, A J Bailey
PMCID: PMC1161363  PMID: 6249253

Abstract

A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 x 10(6)-5 x 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.

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Selected References

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

  1. Bailey A. J., Peach C. M., Fowler L. J. Chemistry of the collagen cross-links. Isolation and characterization of two intermediate intermolecular cross-links in collagen. Biochem J. 1970 May;117(5):819–831. doi: 10.1042/bj1170819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Duance V. C., Restall D. J., Beard H., Bourne F. J., Bailey A. J. The location of three collagen types in skeletal muscle. FEBS Lett. 1977 Jul 15;79(2):248–252. doi: 10.1016/0014-5793(77)80797-7. [DOI] [PubMed] [Google Scholar]
  3. Fraser R. D., MacRae T. P., Suzuki E. Chain conformation in the collagen molecule. J Mol Biol. 1979 Apr 15;129(3):463–481. doi: 10.1016/0022-2836(79)90507-2. [DOI] [PubMed] [Google Scholar]
  4. Gallop P. M., Paz M. A. Posttranslational protein modifications, with special attention to collagen and elastin. Physiol Rev. 1975 Jul;55(3):418–487. doi: 10.1152/physrev.1975.55.3.418. [DOI] [PubMed] [Google Scholar]
  5. Glazer A. N., Sanger F. The iodination of chymotrypsinogen. Biochem J. 1964 Jan;90(1):92–98. doi: 10.1042/bj0900092. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Henkel W., Rauterberg J., Stirtz T. Isolation of a crosslinked cyanogen-bromide peptide from insoluble rabbit collagen. Tissue differences in hydroxylation and glycosylation of the crosslink. Eur J Biochem. 1976 Oct 1;69(1):223–231. doi: 10.1111/j.1432-1033.1976.tb10877.x. [DOI] [PubMed] [Google Scholar]
  7. Light N. D., Bailey A. J. Changes in crosslinking during aging in bovine tendon collagen. FEBS Lett. 1979 Jan 1;97(1):183–188. doi: 10.1016/0014-5793(79)80080-0. [DOI] [PubMed] [Google Scholar]
  8. Light N. D. Bovine type I collagen: A study of cross-linking in various mature tissues. Biochim Biophys Acta. 1979 Nov 23;581(1):96–105. doi: 10.1016/0005-2795(79)90225-3. [DOI] [PubMed] [Google Scholar]
  9. Miller E. J., Robertson P. B. The stability of collagen cross-links when derived from hydroxylsyl residues. Biochem Biophys Res Commun. 1973 Sep 5;54(1):432–439. doi: 10.1016/0006-291x(73)90940-6. [DOI] [PubMed] [Google Scholar]
  10. Parry D. A., Craig A. S., Barnes G. R. Tendon and ligament from the horse: an ultrastructural study of collagen fibrils and elastic fibres as a function of age. Proc R Soc Lond B Biol Sci. 1978 Dec 18;203(1152):293–303. doi: 10.1098/rspb.1978.0106. [DOI] [PubMed] [Google Scholar]
  11. Rauterberg J., Kühn K. Acid soluble calf skin collagen. Characterization of the peptides obtained by cyanogen bromide cleavage of its alpha-1-chain. Eur J Biochem. 1971 Apr;19(3):398–407. doi: 10.1111/j.1432-1033.1971.tb01329.x. [DOI] [PubMed] [Google Scholar]
  12. Robins S. P., Bailey A. J. The chemistry of the collagen cross-links. The characterization of fraction C, a possible artifact produced during the reduction of collagen fibres with borohydride. Biochem J. 1973 Dec;135(4):657–665. doi: 10.1042/bj1350657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Robins S. P., Shimokomaki M., Bailey A. J. The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibres. Biochem J. 1973 Apr;131(4):771–780. doi: 10.1042/bj1310771. [DOI] [PMC free article] [PubMed] [Google Scholar]

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