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  • Title: [Theoretical studies on the influence of binding constants of hemoglobin for ATP and 2,3-diphosphoglycerate on erythrocyte glycolysis].
    Author: Geier T, Glende M, Reich JG.
    Journal: Acta Biol Med Ger; 1978; 37(7):979-92. PubMed ID: 747047.
    Abstract:
    In the red blood cell exist a binding equilibrium of ATP and 2,3-DPG with hemoglobin. For the metabolism only the free active levels of organic phosphates are relevant. The binding constants of hemoglobin increase with decreasing temperature and pH. Using a stoichometric model of glycolysis, the change of free concentrations by altered binding constants and its import on the energy metabolism of the erythrocyte was theoretically studied. The results are: 1. Total ATP-content (bound plus free ATP) does not depend on the binding properties of hemoglobin. 2. Total 2,3-DPG-content is changed by altered binding constants of hemoglobin. The direction of change depends on the ratio energy-consumption/substrate-uptake. 3. In the case of strong binding of organic phosphates to hemoglobin the experimentally measurable total ATP-content does not reflect the free ATP-concentration in the cell water. As a result of binding, free ATP may be low even if total ATP is unchanged. 4. The free concentration of 2,3-DPG always parallels the total content.
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