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Binding of Organic Phosphates to Hemoglobin A and Hemoglobin F

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Book cover Red Cell Metabolism and Function

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 6))

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Abstract

A new physiological system for the regulation of the oxygen affinity to hemoglobin has been discovered during the last two years. Addition of 2,3-diphosphoglycerate (DPG) and adenosine triphosphate (ATP) to dilute hemoglobin solutions dramatically decreased the affinity of the hemoglobin for oxygen (Benesch & Benesch, 1967; Chanutin and Curnish, 1967) and a close inverse relation was found (Akerblom et al., 1968; Engel & Duc, 1968; Lenfant et al., 1968) between the oxygen affinity and the concentration of these phosphocompounds in intact human erythrocytes.

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© 1970 Plenum Press, New York

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Garby, L., de Verdier, CH. (1970). Binding of Organic Phosphates to Hemoglobin A and Hemoglobin F. In: Brewer, G.J. (eds) Red Cell Metabolism and Function. Advances in Experimental Medicine and Biology, vol 6. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3195-7_1

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  • DOI: https://doi.org/10.1007/978-1-4684-3195-7_1

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3197-1

  • Online ISBN: 978-1-4684-3195-7

  • eBook Packages: Springer Book Archive

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