Red-Cell pH and Oxygen Affinity of Hemoglobin

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Abstract
Displacement of the oxyhemoglobin dissociation curve by a change in carbon dioxide tension, discovered in 1904 by Bohr, Hasselbalch and Krogh1 and since named the Bohr effect, is caused by the effect of the concomitant pH change on the hemoglobin molecule. Although this effect of pH is an immediate one, a more sustained effect of pH on the oxygen affinity of hemoglobin also exists.2 , 3 The latter is attributable to the influence of pH on the activity of glycolytic enzymes in the red cells, leading to changed concentrations of certain organic phosphoric compounds, especially 2,3-diphospho-glycerate (2,3-DPG), which has a marked influence . . .