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Identification of Residues responsible for the Alkaline Bohr Effect in Haemoglobin

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Abstract

The imidazole groups of the C-terminal histidines of the β-chains, together with the α-amino groups of the α-chains, are responsible for most of the Bohr effect. In oxyhaemoglobin these groups are free, while in deoxyhaemoglobin their pKs are raised, probably by linkage to carboxyl groups.

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References

  1. Wyman, J., Adv. Protein Chem., 4, 407 (1948).

    Article  CAS  PubMed  Google Scholar 

  2. Kilmartin, J. V., and Rossi-Bernardi, L., Symp. on CO2 (International Union of Physiological Sciences, 1968) (in the press).

    Google Scholar 

  3. Kilmartin, J. V., and Rossi-Bernardi, L., following article, Nature, 222, 1243 (1969).

    Article  ADS  CAS  PubMed  Google Scholar 

  4. Riggs, A., J. Biol. Chem., 236, 1948 (1961).

    CAS  PubMed  Google Scholar 

  5. Benesch, R., and Benesch, R. E., J. Biol. Chem., 236, 405 (1961).

    CAS  Google Scholar 

  6. Smyth, D. G., Battaglia, F. G., and Meschia, G., J. Gen. Physiol., 44, 889 (1961).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Benesch, R. E., and Benesch, R., Biochemistry, 1, 735 (1962).

    Article  CAS  PubMed  Google Scholar 

  8. Morell, S. A., Hoffmann, P., Ayers, V. E., and Taketa, F., Proc. US Nat. Acad. Sci., 48, 1057 (1962).

    Article  ADS  CAS  Google Scholar 

  9. Taylor, J. F., Antonini, E., Brunori, M., and Wyman, J., J. Biol. Chem., 241, 241 (1966).

    CAS  PubMed  Google Scholar 

  10. Perutz, M. F., J. Crystal Growth, 2, 54 (1968).

    Article  ADS  CAS  Google Scholar 

  11. Muirhead, H., Cox, J. M., Mazzarella, L., and Perutz, M. F., J. Mol. Biol., 28, 117 (1967).

    Article  CAS  PubMed  Google Scholar 

  12. Bolton, W., Cox, J. M., and Perutz, M. F., J. Mol. Biol., 33, 283 (1968).

    Article  CAS  PubMed  Google Scholar 

  13. Perutz, M. F., Muirhead, H., Cox, J. M., Goaman, L. C. G., Mathews, F. S., McGandy, E. L., and Webb, L. E., Nature, 219, 29 (1968).

    Article  ADS  CAS  PubMed  Google Scholar 

  14. Perutz, M. F., and Lehmann, H., Nature, 219, 902 (1968).

    Article  ADS  CAS  PubMed  Google Scholar 

  15. Guidotti, G., J. Biol. Chem., 242, 3672 (1967).

    Google Scholar 

  16. Antonini, E., Physiol. Rev., 45, 123 (1965).

    Article  CAS  PubMed  Google Scholar 

  17. Ogawa, S., and McConnell, H. M., Proc. US Nat. Acad. Sci., 58, 19 (1967).

    Article  ADS  CAS  Google Scholar 

  18. Antonini, E., and Brunori, M., J. Biol. Chem., 244, No. 12 (1969).

  19. Antonini, E., Wyman, J., Zito, R., Rossi-Fanelli, A., and Caputo, A., J. Biol. Chem., 236, PC60 (1961).

    CAS  PubMed  Google Scholar 

  20. Zito, R., Antonini, E., and Wyman, J., J. Biol. Chem., 239, 1804 (1964).

    CAS  PubMed  Google Scholar 

  21. Guidotti, G., J. Biol. Chem., 242, 3685 (1967).

    CAS  PubMed  Google Scholar 

  22. Dayhoff, M. O., and Eck, R. V., Atlas of Protein Sequence and Structure (National Biomedical Research Foundation, Silver Spring, 1967–68).

    Google Scholar 

  23. Guidotti, G., J. Biol. Chem., 242, 3685 (1967).

    CAS  PubMed  Google Scholar 

  24. Edelstein, S. J., and Gibson, Q. H. (in the press).

  25. Steinhardt, J., and Beychok, S., in The Proteins (edit. by Neurath, H.), 139 (Academic Press, New York, 1964).

    Google Scholar 

  26. Antonini, A., Schuster, T. M., Brunori, M., and Wynan, J., J. Biol. Chem., 240, PC 2262 (1965).

    CAS  PubMed  Google Scholar 

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PERUTZ, M., MUIRHEAD, H., MAZZARELLA, L. et al. Identification of Residues responsible for the Alkaline Bohr Effect in Haemoglobin. Nature 222, 1240–1243 (1969). https://doi.org/10.1038/2221240a0

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  • DOI: https://doi.org/10.1038/2221240a0

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