Journal of Applied Physiology AJP: Endocrinology and Metabolism
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J Appl Physiol 91: 33-38, 2001;
8750-7587/01 $5.00
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Vol. 91, Issue 1, 33-38, July 2001

Physiological consequences of oxygen-dependent chloride binding to hemoglobin

H. D. Prange1, J. L. Shoemaker Jr.1, E. A. Westen1, D. G. Horstkotte1, and B. Pinshow2

1 Medical Sciences Program, Indiana University, Bloomington, Indiana 47405-7005; and 2 Jacob Blaustein Institute for Desert Research and Department of Life Sciences, Ben-Gurion University of the Negev, Midreshet Ben-Gurion, 84990 Israel

The PO2-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<UP><SUB>3</SUB><SUP>−</SUP></UP>, 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<UP><SUB>3</SUB><SUP>−</SUP></UP> concentration in that compartment.

blood-gas transport; Donnan ratio; Bohr effect; Haldane effect; strong ion difference; bicarbonate; erythrocyte; chloride shift


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