Differences in the Interaction of 2,3-Diphosphoglycerate with Certain Mammalian Hemoglobins

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Science  04 Jun 1971:
Vol. 172, Issue 3987, pp. 1049-1050
DOI: 10.1126/science.172.3987.1049


The hemoglobins of man, horse, dog, rabbit, guinea pig, and rat all have relatively high (nonphysiologic) oxygen affinity when stripped of organic phosphates, and a strong reactivity with 2,3-diphosphoglycerate (2,3-DPG). Appropriately, their red cells contain high levels of 2,3-DPG. In contrast, the sheep, goat, cow, and cat have low oxygen affinity hemoglobins which interact weakly with 2,3-DPG, and low concentrations of red cell 2,3-DPG. These hemoglobins have structural differences at the NH2-terminus of the β chain, a site where 2,3-DPG is thought to bind.

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