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Hemoglobin-oxygen association curves of human erythrocytes were measured in metabolically stable cells under the standardized conditions of extracellular pH 7.400, carbon dioxide tension 38 mmHg (approximately 5 kPa) and temperature 37 degrees C. A model of the oxygen association curve of normal erythrocytes was subsequently developed, based on assumed equilibrium reactions between hemoglobins (Hb), oxygen, and 2,3-diphosphoglycerate (DPG). Conditional equilibrium constants were determined for reactions leading to the formation of species designated Hb-O2 (K = 0.14 mmHg-1), Hb-(O2)4 (K = 0.44 X 10(-4) mmHg-4), Hb-DPG (K = 0.30 X 10(4) L mol-1) and Hb-O2-DPG (K = 0.61 X 10(2) L mol-1 mmHg-1) for unmodified hemoglobin, and Hb-O2 (K = 0.14 mmHg-1) and Hb-(O2)4 (K = 0.44 X 10(-4) mmHg-4) for glycosylated hemoglobin. This model provides a practical means of calculating the expected oxygen association curve for a sample of erythrocytes under standardized conditions, given the intracellular concentrations of hemoglobins and 2,3-diphosphoglycerate and the assumption that the hemoglobins in those cells function normally.
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Ryall et al. (1983) studied this question.
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