PMID: 41712Oct 15, 1979

The pH dependence of the binding of D-glycerate 2,3-bisphosphate to deoxyhemoglobin and oxyhemoglobin. Determination of the number of binding sites in oxyhemoglobin

European Journal of Biochemistry
G G Van Beek, S H de Bruin


The number of Bohr protons released upon oxygenation has been measured over a large range of human hemoglobin concentrations (0.02 to 4.5 mM) in the presence of equimolar amounts of D-glycerate 2,3-bisphosphate. From these data the association constants for the binding of this organic phosphate to deoxyhemoglobin and oxyhemoglobin were calculated at different pH values. The maximum number of protons absorbed upon binding to oxyhemoglobin was determined as well. The maximum number of protons bound to deoxyhemoglobin upon binding of D-glycerate 2,3-bisphosphate was measured independently. From the pH dependence of the association constants and the maximum number of protons absorbed it could be concluded that only one D-glycerate 2,3-bisphosphate can be bound to both deoxyhemoglobin and oxyhemoglobin.


Dec 15, 1975·European Journal of Biochemistry·J BrygierH S Rollema
Apr 1, 1969·Archives of Biochemistry and Biophysics·A Chanutin, E Hermann
Dec 11, 1974·Biochemical and Biophysical Research Communications·B E Hedlund, R Lovrien
Apr 1, 1973·The American Journal of Physiology·C BauerR E Forster
Nov 1, 1973·Biochemical and Biophysical Research Communications·S H de BruinG A van Os
May 7, 1974·Biochemical and Biophysical Research Communications·S H de BruinG A van Os
Sep 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·A Riggs
Jun 1, 1971·Scandinavian Journal of Clinical and Laboratory Investigation·L Garby, C H De Verdier
Jul 1, 1967·Archives of Biochemistry and Biophysics·A Chanutin, R R Curnish
Jan 1, 1964·Advances in Protein Chemistry·J WYMAN

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