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. 1968 Mar;107(1):41–49. doi: 10.1042/bj1070041

Studies on the protein-bound chondroitin sulphate of bovine cortical bone

G M Herring 1
PMCID: PMC1198608  PMID: 5642623

Abstract

A fraction containing chondroitin sulphate, isolated from bovine cortical bone under mild conditions, was separated by ion-exchange chromatography into three fractions with apparent homogeneity on electrophoresis and ultracentrifugation. Two of these appeared to consist of chondroitin sulphate bound to a glycoprotein `core' that had similarities to the bone sialoprotein described previously. The differences in composition of the two fractions were considered to be due to variation in the number or lengths of the polysaccharide chains. The presence of xylose and the alkali-lability of the bond between protein and polysaccharide suggested the presence of a xylosylserine linkage. The third fraction had the properties of a relatively pure chondroitin sulphate which contained a small amount of peptide. These fractions differed considerably from the protein–polysaccharide complexes of epiphysial and other cartilages, and their relevance to the possible role of glycosaminoglycans is discussed.

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Selected References

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

  1. ANDERSON B., HOFFMAN P., MEYER K. THE O-SERINE LINKAGE IN PEPTIDES OF CHONDROITIN 4- OR 6-SULFATE. J Biol Chem. 1965 Jan;240:156–167. [PubMed] [Google Scholar]
  2. ANTONOPOULOS C. A., BORELIUS E., GARDELL S., HAMNSTROM B., SCOTT J. E. The precipitation of polyanions by long-chain aliphatic ammonium compounds. IV. Elution in salt solutions of mucopolysaccharide-quaternary ammonium complexes adsorbed on a support. Biochim Biophys Acta. 1961 Dec 9;54:213–226. doi: 10.1016/0006-3002(61)90360-2. [DOI] [PubMed] [Google Scholar]
  3. ANTONOPOULOS C. A., GARDELL S., SZIRMAI J. A., DETYSSONSK E. R. DETERMINATION OF GLYCOSAMINOGLYCANS (MUCOPOLYSACCHARIDES) FROM TISSUE ON THE MICROGRAM SCALE. Biochim Biophys Acta. 1964 Mar 2;83:1–19. doi: 10.1016/0926-6526(64)90045-x. [DOI] [PubMed] [Google Scholar]
  4. BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
  5. CAMPO R. D., DZIEWIA TKOWSKI D. D. Turnover of the organic matrix of cartilage and bone as visualized by autoradiography. J Cell Biol. 1963 Jul;18:19–29. doi: 10.1083/jcb.18.1.19. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DAVIDSON E., HOFFMAN P., LINKER A., MEYER K. The acid mucopolysaccharides of connective tissue. Biochim Biophys Acta. 1956 Sep;21(3):506–518. doi: 10.1016/0006-3002(56)90188-3. [DOI] [PubMed] [Google Scholar]
  7. DODGSON K. S. Determination of inorganic sulphate in studies on the enzymic and non-enzymic hydrolysis of carbohydrate and other sulphate esters. Biochem J. 1961 Feb;78:312–319. doi: 10.1042/bj0780312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HARTREE E. F. OBSERVATIONS ON THE DETERMINATION OF HEXOSAMINES IN HYDROLYZATES OF GLYCOPROTEINS. Anal Biochem. 1964 Jan;7:103–109. doi: 10.1016/0003-2697(64)90124-1. [DOI] [PubMed] [Google Scholar]
  9. HERRING G. M., KENT P. W. SOME STUDIES ON MUCOSUBSTANCES OF BOVINE CORTICAL BONE. Biochem J. 1963 Dec;89:405–414. doi: 10.1042/bj0890405. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Herring G. M. Studies on the protein-bound chondroitin sulphate of bovine cortical bone. Biochem J. 1967 Aug;104(2):19P–19P. [PMC free article] [PubMed] [Google Scholar]
  11. Hirschman A., Dziewiatkowski D. D. Protein-polysaccharide loss during endochondral ossification: immunochemical evidence. Science. 1966 Oct 21;154(3747):393–395. doi: 10.1126/science.154.3747.393. [DOI] [PubMed] [Google Scholar]
  12. Jibril A. O. Proteolytic degradation of ossifying cartilage matrix and the removal of acid mucopolysaccharides prior to bone formation. Biochim Biophys Acta. 1967 Feb 7;136(1):162–165. doi: 10.1016/0304-4165(67)90335-2. [DOI] [PubMed] [Google Scholar]
  13. KOHN J. A micro-electrophoretic method. Nature. 1958 Mar 22;181(4612):839–840. doi: 10.1038/181839a0. [DOI] [PubMed] [Google Scholar]
  14. KOROTZER J. L., BERGQUIST L. M., SEARCY R. L. Use of cellulose acetate and Ponceau S for electrophoretic serum protein analysis. Am J Med Technol. 1961 Jul-Aug;27:197–203. [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. MALAWISTA I., SCHUBERT M. Chondromucoprotein: new extraction method and alkaline degradation. J Biol Chem. 1958 Jan;230(1):535–544. [PubMed] [Google Scholar]
  17. MUIR H. The nature of the link between protein and carbohydrate of a chondroitin sulphate complex from hyaline cartilage. Biochem J. 1958 Jun;69(2):195–204. doi: 10.1042/bj0690195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Muir H., Jacobs S. Protein-polysaccharides of pig laryngeal cartilage. Biochem J. 1967 May;103(2):367–374. doi: 10.1042/bj1030367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Oldroyd D., Herring G. M. A method for the study of bone mucosubstances by using collagenase. Biochem J. 1967 Aug;104(2):20P–20P. [PMC free article] [PubMed] [Google Scholar]
  20. PARTRIDGE S. M., DAVIS H. F. The chemistry of connective tissues. 4. The presence of a non-collagenous protein in cartilage. Biochem J. 1958 Feb;68(2):298–305. doi: 10.1042/bj0680298. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rodén L., Smith R. Structure of the neutral trisaccharide of the chondroitin 4-sulfate-protein linkage region. J Biol Chem. 1966 Dec 25;241(24):5949–5954. [PubMed] [Google Scholar]
  22. SHATTON J., SCHUBERT M. Isolation of a mucoprotein from cartilage. J Biol Chem. 1954 Dec;211(2):565–573. [PubMed] [Google Scholar]
  23. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  24. VAN DEN HOOFF A. POLYSACCHARIDE HISTOCHEMISTRY OF ENCHONDRAL OSSIFICATION. Acta Anat (Basel) 1964;57:16–28. doi: 10.1159/000142534. [DOI] [PubMed] [Google Scholar]
  25. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
  26. WEATHERELL J. A., WEIDMANN S. M. THE DISTRIBUTION OF ORGANICALLY BOUND SULPHATE IN BONE AND CARTILAGE DURING CALCIFICATION. Biochem J. 1963 Nov;89:265–267. doi: 10.1042/bj0890265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. WEIDMANN S. M. CALCIFICATION OF SKELETAL TISSUES. Int Rev Connect Tissue Res. 1963;1:339–377. doi: 10.1016/b978-1-4831-6755-8.50013-9. [DOI] [PubMed] [Google Scholar]
  28. Williams P. A., Peacocke A. R. The physical properties of a glycoprotein from bovine cortical bone (bone sialoprotein). Biochim Biophys Acta. 1965 Nov 1;101(3):327–335. doi: 10.1016/0926-6534(65)90011-4. [DOI] [PubMed] [Google Scholar]
  29. Williamson M., Vaughan J. Histochemistry of the mucosaccharides in the epiphyseal plate of young rabbits. Nature. 1967 Aug 12;215(5102):711–714. doi: 10.1038/215711a0. [DOI] [PubMed] [Google Scholar]
  30. YEMM E. W., WILLIS A. J. The estimation of carbohydrates in plant extracts by anthrone. Biochem J. 1954 Jul;57(3):508–514. doi: 10.1042/bj0570508. [DOI] [PMC free article] [PubMed] [Google Scholar]

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