Calcified Tissue Research

, Volume 2, Issue 1, pp 253–261 | Cite as

Calcium binding by chondroitin sulfate

  • Marshall R. Urist
  • Donald P. Speer
  • Kenneth J. Ibsen
  • Basil S. Strates
Original Papers


The binding of calcium by chondroitin sulfate C was studied by employing biological and physicochemical methods for the quantitative determination of ionic calcium. Mean values for logKj, the logarithm of the uncorrected formation constant for a calcium-chondroitin sulfate complex, were 1.64 with the frog heart technique, 1.55 with the murexide method, 1.39 with ultrafiltration and 1.04 with the calcium selective electrode. The magnitude of these values suggests that chondroitin sulfate has a relatively high binding capacity for calcium, but calculated values for an exchange parameterKp indicate that calcium has a low affinity for the polysaccharide.

Key words

Calcium Ion Binding Chondroitin Cartilage 


La liaison du calcium par le sulfate de chondroitin C a été étudiée en utilisant des méthodes biologiques et physicochimiques pour la détermination quantitative du calcium ionique. Les valeurs moyennes pour logKj, le logarithme de la constante de formation non corrigée d'un complexe calcium-sulfate de chondroitin C, sont 1,64 par la technique de cœur de grenouille, 1,55 par la méthode de murexide, 1,39 par l'ultrafiltration et 1,04 par l'électrode sélective du calcium. L'ordre de grandeur de ces valeurs suggèrent que le sulfate de chondroitin C a une capacité de liaison pour calcium relativement élevée, mais les valeurs calculées pour un paramètre d'échangeKp indiquent que le calcium a une affinité faible pour le polysaccharide.


Die Bindung von Calcium mit Chondroitinsulfat C wurde untersucht mittels biologischer und physikalisch-chemischer Methoden für die quantitative Bestimmung des ionischen Calciums. Im Durchschnitt ergab logKj, der Logarithmus der unkorrigierten Formationskonstante für einen Calciumchondroitinsulfatkomplex, 1,64 mit der Technik des Froschherzens, 1,55 mit der Murexidmethode, 1,39 mittels Ultrafiltration und 1,04 mit den Calciumselektiven Elektroden. Die Größe dieser Werte zeigt, daß Chondroitinsulfat eine relativ hohe Bindungskapazität für Calcium hat, die berechneten Werte für einen AustauschparameterKp jedoch, daß Calcium eine kleine Affinität für Polysaccharide hat.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bowness, J. M.: Calcium binding by chondroitin sulfate associated with collagen. Biochim. biophys. Acta (Amst.)58, 134–136 (1962).CrossRefGoogle Scholar
  2. —, andK. H. Lee: Effects of chondroitin sulfates on mineralization. Biochem. J.103, 382–390 (1967).PubMedGoogle Scholar
  3. Boyd, E. S., andW. F. Neuman: The surface chemistry of bone. V. The ion-binding properties of cartilage. J. biol. Chem.193, 243–251 (1951).PubMedGoogle Scholar
  4. Buddecke, E., andR. Drzeniek: Stabilitätskonstanten der Calciumkomplexe von sauren Mucopolysacchariden. Hoppe-Seylers physiol. Chem.327, 49–64 (1962).Google Scholar
  5. DiSalvo, J., andM. Schubert: Specific interaction of some protein polysaccharides with freshly precipitating calcium phosphate. J. biol. Chem.242, 705–710 (1967).PubMedGoogle Scholar
  6. Dunstone, J. R.: Some cation-binding properties of cartilage. Biochem. J.72, 465–473 (1959).PubMedGoogle Scholar
  7. — Ion-exchange reactions between cartilage and various cations. Biochem. J.77, 164–170 (1960).PubMedGoogle Scholar
  8. — Ion-exchange reactions between acid mucopolysaccharides and various cations. Biochem. J.85, 336–351 (1962).Google Scholar
  9. Dziewiatkowski, D. D.: The role of sulfated protein-polysaccharide in calcification. Clin. Orthop. Rel. Res.35, 189–201 (1964).Google Scholar
  10. Farber, S. J., andM. Schubert: The binding of cations by chondroitin sulfate. J. clin. Invest.36, 1715–1722 (1957).PubMedGoogle Scholar
  11. Franek, M. D., andJ. R. Dunstone: Connective tissue protein-polysaccharides. Fractionation of the protein-polysaccharides from bovine nasal cartilage. J. biol. Chem.242, 3460–3467 (1967).Google Scholar
  12. Gersh, I., andH. R. Catchpole: The nature of the ground substance of connective tissue. Perspect. Biol. Med.3, 282–320 (1959–1960).Google Scholar
  13. Gilbert, I. G. F., andN. A. Myers: Metal binding properties of chondroitin sulfate. Biochim. biophys. Acta (Amst.)42, 469–475 (1960).CrossRefGoogle Scholar
  14. Harnach, F., andT. B. Coolidge: Determination of ionized calcium in serum with murexide. Analyt. Biochem.6, 477–485 (1963).CrossRefGoogle Scholar
  15. Howell, D. S.: Concepts of calcification. Arthr. and Rheum.6, 736–742 (1963).Google Scholar
  16. Lindenbaum, A., andK. E. Kuettner: Mucopolysaccharides and mucoproteins of calf scapula. Calc. Tiss. Res.1, 153–165 (1967).Google Scholar
  17. McLean, F. C., andA. B. Hastings: The state of calcium in the fluids of the body. I. The conditions affecting the ionization of calcium. J. biol. Chem.108, 285–322 (1935).Google Scholar
  18. Neuman, W. F., E. S. Boyd, andI. Feldman: The ion-binding properties of cartilage. Fourth Conf. Metab. Interrelations, Josiah Macy, Jr., Foundation (N.Y.)4, 100–112 (1952).Google Scholar
  19. Ross, J. W.: Calcium-selective electrode with liquid ion exchanger. Science156, 1378–1379 (1967).PubMedGoogle Scholar
  20. Toribara, T. Y.: Centrifuge type of ultrafiltration apparatus. Analyt. Chem.25, 1286 (1953).CrossRefGoogle Scholar
  21. Urist, M. R. Recent advances in physiology of calcification. J. Bone Jt Surg. A46, 889–900 (1964).Google Scholar
  22. —, andJ. L. Abernethy: Effects of the calcium ion upon structure and calcificability of tendon. Clin. Orthop. Rel. Res.51, 255–274 (1967).Google Scholar
  23. —, andJ. M. Adams, Jr.: Effect of various blocking reagents upon local mechanism of calcification. Arch. Path.81, 325–342 (1966).PubMedGoogle Scholar
  24. —, andJ. M. Adams, Jr.: Calcification of tendon: A triphasic local mechanism. Arch. Path.77, 594–608 (1964).PubMedGoogle Scholar
  25. —, andF. C. McLean: Calcium oxytetracycline complexes. New apparatus for frog heart method of estimation of calcium ion concentration. Proc. Soc. exp. Biol. (N.Y.)109, 801–804 (1962).Google Scholar
  26. Weinstock, A., P. C. King, andR. E. Wuthier: The ion-binding characteristics of reconstituted collagen. Biochem. J.102, 983–988 (1967).Google Scholar

Copyright information

© Springer-Verlag 1968

Authors and Affiliations

  • Marshall R. Urist
    • 1
  • Donald P. Speer
    • 1
  • Kenneth J. Ibsen
    • 1
  • Basil S. Strates
    • 1
  1. 1.Bone Research Laboratory, School of MedicineUniversity of CaliforniaLos Angeles

Personalised recommendations