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Original Article

Effects of Some Organic Phosphate Compounds on the Oxyhemoglobin Dissociation Curve in Human Erythrolysate

Pages 208-210 | Received 18 Sep 1968, Accepted 01 Oct 1968, Published online: 05 Aug 2009

References

  • Astrup P., Engel K., Severinghaus J. W., Munson E. The influence of temperature and pH on the dissociation curve of oxyhemoglobin of human blood. Scand. J. clin. Lab. Invest. 1965; 17: 515
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  • Benesch R., Benesch R. E. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. bio-phys. Res. Commun. 1967; 26: 162
  • Benesch R., Benesch R. E. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Nat. Acad. Sci. 1968; 59: 526
  • Chanutin A., Curnish R. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocyte. Arch. Biochem. Biophys. 1967; 121: 96
  • Garby L., De Verdier C.-H. Binding of ATP and 2.3–DPG to hemoglobin-effect on erythrocyte glycolysis. Folia Haematologica 1968; 89: 421
  • Garby L., Gerber G., De Verdier C.-H. Binding of 2.3–diphosphoglycerate and adenosine triphosphate to human hemoglobin, In manuscript.
  • Hill A. V. The possible effect of the aggregation of the molecules of hemoglobin on its dissociation curves. J. Physiol. 1910; 40: IV–VII
  • Siggaard-Andersen O., Jörgensen K., Neraa N. Spectrophotometric determination of oxygen saturation in capillary blood. Scand. J. clin. Lab. Invest. 1962; 14: 298

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