Abstract
THERE is a decrease in the O2 affinity of mammalian haemoglobin (Hb) as the levels of 2,3-DPG or ATP are increased, which is explained by an allosteric effect on the HbO2 binding1,2. Similar observations on amphibians3 and fish4, which have molar ratios of ATP to Hb similar to those of DPG to Hb in mammals, suggest that red cell organic phosphates modulate Hb function in all vertebrates. The adaptation of mammals to various hypoxic stresses involves reduced HbO2 affinity5–9, the attendant increase in O2 “unloading” capacity being mediated by an increase in the concentration of red cell 2,3-DPG. We have found the opposite response in hypoxic fish and suggest that an increased O2 affinity results in increased O2 transport for the fish.
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WOOD, S., JOHANSEN, K. Adaptation to Hypoxia by Increased HbO2 Affinity and Decreased Red Cell ATP Concentration. Nature New Biology 237, 278–279 (1972). https://doi.org/10.1038/newbio237278a0
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DOI: https://doi.org/10.1038/newbio237278a0
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