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Effect of 2,3-diphosphoglycerate on the cooperativity in oxygen binding of human adult hemoglobin

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
43
Issue
2
Identifiers
DOI: 10.1016/0006-291x(71)90770-4

Abstract

Abstract Oxygen equilibrium curves of human adult hemoglobin (Hb A) have been analysed by the Scatchard and Hill plots and four successive association constants for the binding of oxygen have been determined by fitting the polts with simulated curves calculated by a digital computer. 2,3-Diphosphoglycerate (DPG) markedly reduces the affinity of Hb A to the 1st, 2nd, and 3rd molecules of oxygen without affecting the affinity to the 4th molecule, which is similar to the oxygen affinity of the isolated β chains. Thus, the over-all free energy of interaction increases by about 1400 cal per site and the maximum slope of the Hill plot, n, increases significantly in the presence of 2 × 10 −3 M DPG.

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