Differences in the interaction of 2, 3-diphosphoglycerate with certain mammalian hemoglobins
HF Bunn - Science, 1971 - science.org
HF Bunn
Science, 1971•science.orgThe 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 …
(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 …
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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