Analysis of the interaction of organic phosphates with hemoglobin

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Abstract
A model-independent analysis was employed to evaluate the accuracy of Adair constants determined in the presence of 2,3-diphosphoglycerate (DPG). The change of O2 affinity in the presence of phosphates was related to the macroscopic phosphate binding constants of oxy- and deoxyhemoglobin and used to extract such binding constants from O2 equilibrium measurements. The change of the Bofr effect in the presence of phosphates and the competitive binding of CO2 and DPG were treated quantitatively. The binding of organic phosphates was incorporated into an allosteric model, in which the effect of phosphate on both tertiary and quaternary structure changes was included. By use of this model, the factors which can be responsible for the increased functional heterogeneity of .alpha. and .beta. chains in the presence of phosphates were clarified.

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