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Science 4 June 1971:
Vol. 172. no. 3987, pp. 1049 - 1050
DOI: 10.1126/science.172.3987.1049
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Articles

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

H. Franklin Bunn 1

1 Thorndike Memorial Laboratory, Boston City Hospital, Boston, Massachusetts 02118

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 beta chain, a site where 2,3-DPG is thought to bind.


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