Oxygen uptake by the blood in the lungs of a resting human brings the level of saturation of haemoglobin from ∼70% to >97% (refs 1,2). The recourse to this upper portion of the oxygen binding curve is reflected in an asymmetry of the isotherm which is frequently reported3,4, but which has not been accorded any physiological role. This asymmetry is responsible for a more pronounced cooperativity of the deoxygenation at nearly complete saturation than that displayed in the typical sigmoidal pattern of loading at low oxygen tensions. Such behaviour is viewed here as a consequence of and a possible rationalization for the presence of two similar but distinct types of subunit in the haemoglobin tetramer.
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Peller, L. Cooperative deoxygenation of haemoglobin: asymmetry of binding and subunit differences. Nature 300, 661–662 (1982). https://doi.org/10.1038/300661a0
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