Summary
The Haldane coefficient (the amount of the oxygen-linked hydrogen ion binding of hemoglobin) was determined in bovine erythrolysate (Hb concentration=13.5 mM) by means of the differential titration method with varying PCO2 from 0 to 74 mm Hg and pH from 6.0 to 8.5 at 37°C. The maximum value of the coefficient was found to be 0.49 mM per mM Hb at PCO2=0 and pH 7.20. With increasing of PCO2, the coefficient became smaller in all ranges of pH studied. The coefficient under the conditions of pH 7.20 and PCO2=45 mm Hg that are normally prevailing in the interior of bovine erythrocytes was 0.31.
Similar content being viewed by others
References
O. Siggaard-Andersen, Scand. J. clin Lab. Invest.27, 351 (1971).
O. Siggaard-Andersen,The Acid-Base Status of the Blood, 4th edn. (Munksgaard, Copenhagen 1974), p. 79.
N. Takano, E. Hayashi andK. Matsue, Clin. Physiol.5, 357 (1975), in Japanese.
J. D. Torrance, inErythrocytes, Thrombocytes, Leukocytes. (Ed.E. Gerlach; Georg Thieme Publ., Stuttgart 1973), p. 161.
L. H. van Kempen, P. M. Breepoel andF. Kreuzer, Respir. Physiol.23, 223 (1975).
H. F. Bunn, Science.172, 1049 (1971).
S. H. de Bruin, L. H. M. Janssen andG. A. J. van Os, Biochim. biophys. Acta188, 207 (1969).
K. A. Evelyn andH. T. Malloy, J. biol. Chem.126, 655 (1938).
N. Takano, E. Hayashi andK. Matsue, Pflügers Archiv, in press.
J. V. Kilmartin andL. Rossi-Bernardi, Physiol. Rev.53, 836 (1973).
L. Garby, M. Robert andB. Zaar, Acta physiol. scand.84, 482 (1972).
Author information
Authors and Affiliations
Additional information
Acknowledgments. We are much obliged to Dr.J. N. Hunt for his valuable discussion during preparation of the manuscript.
Rights and permissions
About this article
Cite this article
Takano, N., Nishikura, K. The oxygen-linked hydrogen ion binding (the Haldane coefficient) of bovine hemoglobin. Experientia 32, 1437–1439 (1976). https://doi.org/10.1007/BF01937419
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF01937419