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Carbonate: Key to Transferrin Chemistry

  • George W. Bates
  • Gary Graham
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

Transferrin, the serum iron transport protein, has three important functions. First, to sequester iron; second, to transport it in a form that is nontoxic and unavailable to the nonspecific complexing agents of serum; and third, to release iron to specific receptor sites on cell membranes. The chemistry of transferrin is a reflection of these physiological functions. Current topics in transferrin research are presented in the proceedings of the recent European Biology Organization Workshop on Iron Proteins (1).

Keywords

Binary Complex Metal Binding Site Iron Release Iron Removal Apparent Dissociation Constant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Bibliography

  1. 1.
    Crichton, R. R., Ed. (1974) Proteins of Iron Storage and Transport; Proceedings of the EMBO Symposium, ASP Biological and Medical Press, AmsterdamGoogle Scholar
  2. 2.
    Bates, G. W., and Schlabach, M. R. (1975) J. Biol. Chem. 250, 2177–2181PubMedGoogle Scholar
  3. 3.
    Aasa, R., and Aisen, P. (1968) J. Biol. Chem. 243, 2399–2404PubMedGoogle Scholar
  4. 4.
    Bates, G. W., and Schlabach, M. R. (1974) The Synergistic Binding of Metal Ions and Anions by Transferrin in Proteins of Iron Storage and Transport; Proceedings of the EMBO Symposium, R. R. Crichton, Ed., ASP Biological and Medical Press, AmsterdamGoogle Scholar
  5. 5.
    Schlabach, M. R., and Bates, G. W. (1975) J. Biol. Chem. 250, 2182–2188PubMedGoogle Scholar
  6. 6.
    Martinez-Medellin, J. and Schulman, H. M. (1972) Biochim. Biophys. Acta 264, 272–284PubMedCrossRefGoogle Scholar
  7. 7.
    Price, E. M. and Gibson, J. F. (1972) Biochem. Biophys. Res. Commun. 46, 646–651PubMedCrossRefGoogle Scholar
  8. 8.
    Phelps, C. F. and Antonini, E. (1975) Biochem. J. 147, 385–391PubMedGoogle Scholar
  9. 9.
    Jandl, J., Inman, J., Simmons, R., and Allen, D. (1959) J. Clin. Invest. 38, 161–185PubMedCrossRefGoogle Scholar
  10. 10.
    Bates, G. W., Billups, C. and Saltman, P. (1967) J. Biol. Chem. 242, 2816–2821PubMedGoogle Scholar
  11. 11.
    Johnston, D. O., and Cottingham, A. B. (1969) Biochim. Biophys. Acta 177, 113–117PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • George W. Bates
    • 1
  • Gary Graham
    • 1
  1. 1.Department of Biochemistry and Biophysics, Texas Agricultural Experiment StationTexas A&M UniversityCollege StationUSA

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