Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Jan 1;185(1):195–201. doi: 10.1042/bj1850195

Identification of cyanogen bromide peptides involved in intermolecular cross-linking of bovine type III collagen.

A C Nicholls, A J Bailey
PMCID: PMC1161284  PMID: 6769428

Abstract

Cyanogn bromide peptides derived from bovine type III collagen and containing reducible cross-links were isolated and identified. Two peptides, alpha 1 (III)CB7 and alpha 1 (III)CB9B, from within the helical portion of the molecule were shown to contain the 'amino donor' residues cross-linked to non-helical 'aldehyde donor' residues in the formation of cross-links. This information, in conjunction with previously published data for the order of the cyanogen bromide peptides [Fietzek, Allman, Rauterberg & Wachter (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 84-86], suggests that in type III collagen intermolecular cross-links are located in the end-overlap regions, so as to stabilize a quarter-stagger arrangement of molecules within the fibre in a similar manner to that proposed for type I and type II collagens.

Full text

PDF
200

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. Bailey A. J., Sims T. J. Chemistry of the collagen cross-links. Nature of the cross-links in the polymorphic forms of dermal collagen during development. Biochem J. 1976 Feb 1;153(2):211–215. doi: 10.1042/bj1530211. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Becker U., Fietzek P. P., Nowack H., Timpl R. Isolation and structure of the amino-terminal cross-linking region in insoluble type III collagen. Hoppe Seylers Z Physiol Chem. 1976 Dec;357(10):1409–1415. doi: 10.1515/bchm2.1976.357.2.1409. [DOI] [PubMed] [Google Scholar]
  4. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  5. Chung E., Miller E. J. Collagen polymorphism: characterization of molecules with the chain composition (alpha 1 (3)03 in human tissues. Science. 1974 Mar;183(130):1200–1201. doi: 10.1126/science.183.4130.1200. [DOI] [PubMed] [Google Scholar]
  6. De Luque O., Mechanic G., Tanzer M. L. Isolation of peptides containing the cross-link, hydroxylysinonorleucine, from reconstituted collagen fibrils. Biochemistry. 1970 Dec 8;9(25):4987–4993. doi: 10.1021/bi00827a024. [DOI] [PubMed] [Google Scholar]
  7. Dixit S. N., Bensusan H. B. The isolation of crosslinked peptides of collagen involving alpha 1-CB6. Biochem Biophys Res Commun. 1973 May 1;52(1):1–8. doi: 10.1016/0006-291x(73)90945-5. [DOI] [PubMed] [Google Scholar]
  8. Epstein E. H., Jr, Munderloh N. H. Isolation and characterization of CNBr peptides of human (alpha 1 (III) )3 collagen and tissue distribution of (alpha 1 (I) )2 alpha 2 and (alpha 1 (III) )3 collagens. J Biol Chem. 1975 Dec 25;250(24):9304–9312. [PubMed] [Google Scholar]
  9. Eyre D. R., Glimcher M. J. Collagen cross-linking. Isolation of cross-linked peptides from collagen of chicken bone. Biochem J. 1973 Nov;135(3):393–403. doi: 10.1042/bj1350393. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fietzek P. P., Allmann H., Rauterberg J., Wachter E. Ordering of cyanogen bromide peptides of type III collagen based on their homology to type I collagen: preservation of sites for crosslink formation during evolution. Proc Natl Acad Sci U S A. 1977 Jan;74(1):84–86. doi: 10.1073/pnas.74.1.84. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fujii K., Corcoran D., Tanzer M. L. Isolation and structure of a cross-linked tripeptide from calf bone collagen. Biochemistry. 1975 Oct 7;14(20):4409–4413. doi: 10.1021/bi00691a011. [DOI] [PubMed] [Google Scholar]
  12. Fujii K., Tanzer M. L. Aldehyde content and cross-linking of type III collagen. Biochem Biophys Res Commun. 1976 Mar 8;69(1):128–134. doi: 10.1016/s0006-291x(76)80282-3. [DOI] [PubMed] [Google Scholar]
  13. Fujii T., Kühn K. Isolation and characterization of pepsin-treated type III collagen from calf skin. Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1793–1801. doi: 10.1515/bchm2.1975.356.2.1793. [DOI] [PubMed] [Google Scholar]
  14. Furthmayr H., Timpl R. Characterization of collagen peptides by sodium dodecylsulfate-polyacrylamide electrophoresis. Anal Biochem. 1971 Jun;41(2):510–516. doi: 10.1016/0003-2697(71)90173-4. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Kang A. H. Studies on the location of intermolecular cross-links in collagen. Isolation of a CNBr peptide containing -hydroxylysinonorleucine. Biochemistry. 1972 May 9;11(10):1828–1835. doi: 10.1021/bi00760a015. [DOI] [PubMed] [Google Scholar]
  17. Miller E. J. Collagen cross-linking: identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagen. Biochem Biophys Res Commun. 1971 Oct 15;45(2):444–451. doi: 10.1016/0006-291x(71)90839-4. [DOI] [PubMed] [Google Scholar]
  18. Piez K. A. Molecular weight determination of random coil polypeptides from collagen by molecular sieve chromatography. Anal Biochem. 1968 Nov;26(2):305–312. doi: 10.1016/0003-2697(68)90342-4. [DOI] [PubMed] [Google Scholar]
  19. Rauterberg J., Allmann H., Henkel W., Fietzek P. P. Isolation and characterization of CNBr derived peptides of the alpha1 (III) chain of pepsin-solubilized calf skin collagen. Hoppe Seylers Z Physiol Chem. 1976 Dec;357(10):1401–1407. doi: 10.1515/bchm2.1976.357.2.1401. [DOI] [PubMed] [Google Scholar]
  20. Scott P. G., Veis A., Mechanic G. The identity of a cyanogen bromide fragment of bovine dentin collagen containing the site of an intermolecular cross-link. Biochemistry. 1976 Jul 27;15(15):3191–3198. doi: 10.1021/bi00660a006. [DOI] [PubMed] [Google Scholar]
  21. Sykes B. C., Bailey A. J. Molecular weight heterogeneity of the alpha-chain sub-units of collagen. Biochem Biophys Res Commun. 1971 Apr 16;43(2):340–345. doi: 10.1016/0006-291x(71)90758-3. [DOI] [PubMed] [Google Scholar]
  22. Timpl R., Glanville R. W., Nowack H., Wiedemann H., Fietzek P. P., Kühn K. Isolation, chemical and electron microscopical characterization of neutral-salt-soluble type III collagen and procollagen from fetal bovine skin. Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1783–1792. doi: 10.1515/bchm2.1975.356.2.1783. [DOI] [PubMed] [Google Scholar]
  23. Zimmermann B. K., Timpl R., Kühn K. Intermolecular cross-links of collagen. Participation of the carboxy-terminal nonhelical region of the 1-chain. Eur J Biochem. 1973 Jun;35(2):216–221. doi: 10.1111/j.1432-1033.1973.tb02828.x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES