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

H. Franklin Bunn
Science
New Series, Vol. 172, No. 3987 (Jun. 4, 1971), pp. 1049-1050
Stable URL: http://www.jstor.org/stable/1732339
Page Count: 2
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Abstract

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 NH$_{2}$-terminus of the β chain, a site where 2,3-DPG is thought to bind.

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