Physiological consequences of oxygen-dependent chloride binding to hemoglobin
2001
The Po 2-dependent binding of chloride to Hb decreases the Cl− concentration of the red blood cell (RBC) intracellular fluid in venous blood to ∼1–3 mmol/l less than that in arterial blood. This change is physiologically important because 1 ) Cl− is a negative heterotropic allosteric effector of Hb that competes for binding sites with 2,3-bisphosphoglycerate and CO2 and decreases oxyhemoglobin affinity in several species; 2 ) it may help reconcile several longstanding problems with measured values of the Donnan ratios for Cl−, HCO 3 − , and H+ across the RBC membrane that are used to calculate total CO2 carriage, ion flux rates, and membrane potentials; 3 ) it is a factor in the change in the dissociation constant for the combined nonvolatile weak acids of Hb associated with the Haldane effect; and 4 ) it diminishes the decrease in strong ion difference in the RBC intracellular fluid that would otherwise occur from the chloride shift and prevent the known increase of HCO 3 − concentration in that compartment.
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