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. 1976 Dec 1;159(3):749–755. doi: 10.1042/bj1590749

A comparison of bone matrix and tendon with particular reference to glycoprotein content.

G M Herring
PMCID: PMC1164178  PMID: 188411

Abstract

Bone matrix and tendon are compared in terms of their carbohydrate and non-collagenous protein composition. The collagen content of both tissues was similar (90-91%), but bone matrix had at least three times as much sialic acid (0.28%) as tendon (0.08%). Smaller differences were found in the analysis of hexoses and hexosamines. After digestion with bacterial collagenase, about 9% of the total protein from both tissues was non-diffusible on dialysis, and this contained only 0.15% (bone) and 0.7% (tendon) of the original hydroxyproline; recovery of sialic acid was 86-87%. The collagenase-resistant soluble material amounted to about 9% (bone matrix) and 5% (tendon); the insoluble residues were 1 and 4% respectively. There were clear differences in the carbohydrate contents of the digests, but the amino acid compositions were similar. When the soluble digests were chromatographed on DEAE-cellulose, the elution profiles indicated the presence in each tissue of a variety of glycoproteins and a proteoglycan fraction, and showed clearly that an acidic glycoprotein corresponding to bone sialoprotein was not present in tendon.

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Selected References

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

  1. AMINOFF D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J. 1961 Nov;81:384–392. doi: 10.1042/bj0810384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson J. C. Glycoproteins of the connective tissue matrix. Int Rev Connect Tissue Res. 1976;7:251–322. doi: 10.1016/b978-0-12-363707-9.50012-5. [DOI] [PubMed] [Google Scholar]
  3. Anderson J. C. Isolation of a glycoprotein and proteodermatan sulphate from bovine achilles tendon by affinity chromatography on concanavalin A-Sepharose. Biochim Biophys Acta. 1975 Feb 27;379(2):444–455. doi: 10.1016/0005-2795(75)90151-8. [DOI] [PubMed] [Google Scholar]
  4. Anderson J. C., Jackson D. S. The isolation of glycoproteins from bovine achilles tendon and their interaction with collagen. Biochem J. 1972 Mar;127(1):179–186. doi: 10.1042/bj1270179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Andrews A. T., Herring G. M., Kent P. W. Some studies on the composition of bovine cortical-bone sialoprotein. Biochem J. 1967 Sep;104(3):705–715. doi: 10.1042/bj1040705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Andrews A. T., Herring G. M., Kent P. W. The periodate oxidation of bovine bone sialoprotein, and some observations on its structure. Biochem J. 1969 Mar;111(5):621–627. doi: 10.1042/bj1110621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ashton B. A., Triffitt J. T., Herring G. M. Isolation and partial characterization of a glycoprotein from bovine cortical bone. Eur J Biochem. 1974 Jun 15;45(2):525–533. doi: 10.1111/j.1432-1033.1974.tb03577.x. [DOI] [PubMed] [Google Scholar]
  8. Benya P., Berger K., Golditch M., Schneir M. Recommendations concerning the use of bacterial collagenase for isolating collagen-associated molecules from tissues. Anal Biochem. 1973 May;53(1):313–316. doi: 10.1016/0003-2697(73)90438-7. [DOI] [PubMed] [Google Scholar]
  9. Buscher H. P., Casals-Stenzel J., Schaufer R. New sialic acids. Identification of N-glycoloyl-O-acetylneuraminic acids and N-acetyl-O-glycoloylneuraminic acids by improved methods for detection of N-acyl and O-acyl groups and by gas-liquid chromatography. Eur J Biochem. 1974 Dec 16;50(1):71–82. doi: 10.1111/j.1432-1033.1974.tb03873.x. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Dorner R. W., Antonopoulos C. A., Gardell S. Application of cetylpyridinium-complex elution methods to analysis of glycosaminoglycans of tendon. Biochim Biophys Acta. 1968 Jun 24;158(3):336–343. doi: 10.1016/0304-4165(68)90287-0. [DOI] [PubMed] [Google Scholar]
  12. Gatt R., Berman E. R. A rapid procedure for the estimation of amino sugars on a micro scale. Anal Biochem. 1966 Apr;15(1):167–171. doi: 10.1016/0003-2697(66)90262-4. [DOI] [PubMed] [Google Scholar]
  13. Grant M. E., Jackson D. S. Carbohydrate content of bovine collagen preparations. Biochem J. 1968 Jul;108(4):587–591. doi: 10.1042/bj1080587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. HERRING G. M. COMPARISON OF BOVINE BONE SIALOPROTEIN AND SERUM OROSOMUCOID. Nature. 1964 Feb 15;201:709–709. doi: 10.1038/201709a0. [DOI] [PubMed] [Google Scholar]
  15. Hamilton R. H. A direct photometric method for chloride in biological fluids, employing mercuric thiocyanate and perchloric acid. Clin Chem. 1966 Jan;12(1):1–17. [PubMed] [Google Scholar]
  16. Herring G. M., Ashton B. A. The isolation of soluble proteins, glycoproteins, and proteoglycans from bone. Prep Biochem. 1974;4(2):179–200. doi: 10.1080/00327487408068771. [DOI] [PubMed] [Google Scholar]
  17. KOHN J. A micro-electrophoretic method. Nature. 1958 Mar 22;181(4612):839–840. doi: 10.1038/181839a0. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. Lee-Own V., Anderson J. C. The preparation of a bacterial collagenase containing negligible non-specific protease activity. Prep Biochem. 1975;5(3):229–245. doi: 10.1080/00327487508061574. [DOI] [PubMed] [Google Scholar]
  20. MANDL I., ZIPPER H., FERGUSON L. T. Clostridium histolyticum collagenase: its purification and properties. Arch Biochem Biophys. 1958 Apr;74(2):465–475. doi: 10.1016/0003-9861(58)90017-1. [DOI] [PubMed] [Google Scholar]
  21. Nakajima O., Gray C. H. Studies on haem alpha-methenyl oxygenase. Isomeric structure of formylbiliverdin, a possible precursor of biliverdin. Biochem J. 1967 Jul;104(1):20–22. doi: 10.1042/bj1040020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ochsenfahrt H., Winne D. Intestinal blood flow and drug absorption from the rat jejunum. Life Sci. 1968 May 1;7(9):493–498. doi: 10.1016/0024-3205(68)90052-0. [DOI] [PubMed] [Google Scholar]
  23. Peacocke A. R., Williams P. A. The binding of hydrogen ions to an acidic glycoprotein from bovine cortical bone. Biochem J. 1967 Dec;105(3):1171–1175. doi: 10.1042/bj1051171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Peterkofsky B., Diegelmann R. Use of a mixture of proteinase-free collagenases for the specific assay of radioactive collagen in the presence of other proteins. Biochemistry. 1971 Mar 16;10(6):988–994. doi: 10.1021/bi00782a009. [DOI] [PubMed] [Google Scholar]
  25. Porter W. H., Cunningham L. W., Mitchell W. M. Studies on the active site of clostripain. The specific inactivation by the chloromethyl ketone derived from -N-tosyl-L-lysine. J Biol Chem. 1971 Dec 25;246(24):7675–7682. [PubMed] [Google Scholar]
  26. Timpl R., Wolff I., Weiser M. Acidic structural proteins of connective tissue. I. Solubilization and preliminary chemical characterization. Biochim Biophys Acta. 1969 Nov 11;194(1):112–120. doi: 10.1016/0005-2795(69)90186-x. [DOI] [PubMed] [Google Scholar]
  27. Triffitt J. T., Owen M. Studies on bone matrix glycoproteins. Incorporation of (1-14C)glucosamine and plasma (14C)glycoprotein into rabbit cortical bone. Biochem J. 1973 Sep;136(1):125–134. doi: 10.1042/bj1360125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. WERNER I., ODIN L. On the presence of sialic acid in certain glycoproteins and in gangliosides. Acta Soc Med Ups. 1952;57(3-4):230–241. [PubMed] [Google Scholar]
  29. Williams P. A., Peacocke A. R. The binding of calcium and yttrium ions to a glycoprotein from bovine cortical bone. Biochem J. 1967 Dec;105(3):1177–1185. doi: 10.1042/bj1051177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. 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]
  31. Wolff I., Fuchswans W., Weiser M., Furthmayr H., Timpl R. Acidic structural proteins of connective tissue. Characterization of their heterogeneous nature. Eur J Biochem. 1971 Jun 11;20(3):426–431. doi: 10.1111/j.1432-1033.1971.tb01409.x. [DOI] [PubMed] [Google Scholar]

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