Abstract
IT has been reported by several authors that human hæmoglobin dissociates into sub-units in strong salt solutions (that is, in sodium chloride above 0.5 M). The decrease of molecular weight of hæmoglobin in such conditions was demonstrated by sedimentation1,2, osmotic-pressure3 and light-scattering4 methods. According to present views5 on the oxygen equilibrium of mammalian hæmoglobins, the decrease in the molecular weight of hæmoglobin (and therefore the decrease in the number of the oxygen-combining centres per molecule) should be accompanied by alterations of the shape of the oxygen equilibrium curve. Taking the value of n in the Hill empirical equation: 
as a measure of the sigmoid character of the curve, this value should be lower than 2 for a splitting of hæmoglobin into halves5.
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References
Svedberg, T., and Pedersen, K. O., “The Ultracentrifuge” (Oxford, 1940).
Rossi-Fanelli, A., Caputo, A., and Antonini, E. (unpublished experiments).
Gutfreund, H., “Hæmoglobin” (Butterworths Sci. Pub., London, 1949).
Benhamou, N., and Weill, G., Biochim. Biophys. Acta, 24, 548 (1957).
Wyman, J., “Adv. Protein Chem.”, 4, 407 (1948).
Rossi-Fanelli, A., and Antonini, E., Arch. Biochem. Biophys., 77, 478 (1958).
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ROSSI-FANELLI, A., ANTONINI, E. & CAPUTO, A. Oxygen Equilibrium of Human Hæmoglobin in Strong Salt Solutions. Nature 183, 827–828 (1959). https://doi.org/10.1038/183827a0
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DOI: https://doi.org/10.1038/183827a0
