Section II. Binding of Organic Phosphates to Hemoglobin

References

• Sugita Y., Chanutin A. Electrophoretic studies of red cell hemolysates supplemented with phosphorylated carbohydrate intermediates. Proc. Soc. Exp. Biol. Med. 1963; 112: 72
   PubMed Web of Science ®Google Scholar
• Benesch R., Benesch R. E. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Commun. 1967; 26: 162
   PubMed Web of Science ®Google Scholar
• Chanutin A., Curnish R. R. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes. Arch. Biochem. Biophys. 1967; 121: 96
   PubMed Web of Science ®Google Scholar
• Benesch R., Benesch R. E. Intracellular organic phosphates as regulators of oxygen release by haemoglobin. Nature 1969; 221: 618
   PubMed Web of Science ®Google Scholar
• Adair G. S., Barcroft J., Bock A. V. The identity of haemoglobin in human beings. J. Physiol. 1921; 55: 322
   PubMedGoogle Scholar
• Rapoport S., Guest G. M. Distribution of acid-soluble phosphorus in the blood cells of various vertebrates. J. Biol. Chem. 1941; 138: 269
   Google Scholar
• Bartlett G. R., Barnet H. N. Changes in the phosphate compounds of the human red blood cell during blood bank storage. J. Clin. Invest. 1960; 39: 56
   PubMed Web of Science ®Google Scholar
• Berry E. R., Chanutin A. Electrophoretic studies of red cell extracts of stored blood. J. Clin. Invest. 1957; 36: 225
   PubMedGoogle Scholar
• Chanutin A., Curnish R. R. Factors influencing the electrophoretic patterns of red cell hemolyzates analyzed in cacodylate buffers. Arch. Biochem. Biophys. 1964; 106: 433
   PubMed Web of Science ®Google Scholar
• Benesch R., Benesch R. E., Yu C. I. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Nat. Acad. Sci. USA 1968; 59: 526
   PubMed Web of Science ®Google Scholar
• Benesch R. E., Benesch R., Yu C. I. The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. Biochemistry 1969; 8: 2567
   PubMed Web of Science ®Google Scholar
• Luque J., Diederich D., Grisolia S. Binding of 2,3-diphosphoglycerate to oxyhemoglobin. Biochem. Biophys. Res. Commun. 1969; 36: 1019
   PubMed Web of Science ®Google Scholar
• Edwards M. J., Rigas D. A. Electrolyte-labile increase of oxygen affinity during the in vivo aging of hemoglobin. J. Clin. Invest. 1967; 46: 1579
   PubMedGoogle Scholar
• Bernstein R. E. Alterations in metabolic energetics and cation transport during aging of red cells. J. Clin. Invest. 1959; 38: 1572
   PubMed Web of Science ®Google Scholar
• Shojania A. M., Israels L. G., Zipursky A. The relationship of adenine triphosphate concentration to erythrocyte aging. J. Lab. Clin. Med. 1968; 71: 41
   PubMedGoogle Scholar
• Benesch R., Benesch R. E., Enoki Y. The interaction of hemoglobin and its subunits with 2,3-diphosphoglycerate. Proc. Nat. Acad. Sci. USA 1968; 61: 1102
   PubMedGoogle Scholar
• Garby L., Gerber G., de Verdier C.-H. Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human haemoglobin A. Europ. J. Biochem. 1969; 10: 110
   PubMedGoogle Scholar
• Perutz M. F., Muirhead H., Cox J. M., Goaman L. C. G. Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: (II) The atomic model. Nature 1968; 219: 131
   PubMed Web of Science ®Google Scholar
• Bolton W., Cox J. M., Perutz M. F. Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 Å resolution. J. Molec. Biol. 1968; 33: 283
   PubMedGoogle Scholar
• de Verdier C.-H., Garby L. Low binding of 2,3-diphosphoglycerate to haemoglobin F. A contribution to the knowledge of the binding site and an explanation for the high oxygen affinity of foetal blood. Scand. J. Clin. Lab. Invest. 1969; 23: 149
   PubMed Web of Science ®Google Scholar
• Chanutin A., Curnish R. R. Effect of organic phosphates on the oxygen equilibrium of carboxypeptidase digests of human hemoglobin. Arch. Biochem. Biophys. 1968; 123: 163
   PubMed Web of Science ®Google Scholar
• Schruefer J. J. P., Heller C. J., Battaglia F. C., Hellegers A. E. Independence of whole blood and haemoglobin oxygen dissociation curves from haemoglobin type. Nature 1962; 196: 550
   PubMed Web of Science ®Google Scholar
• Nechtman C. M., Huisman T. H. J. Comparative studies of oxygen equilibria of human adult and cord blood red cell hemolysates and suspensions. Clin. Chim. Acta 1964; 10: 165
   PubMed Web of Science ®Google Scholar
• Delivoria-Papadopoulos M., Oski F. A., Gottlieb A. J. Oxygen-hemoglobin dissociation curves: effect of inherited enzyme defects of the red cell. Science 1969; 165: 601
   PubMed Web of Science ®Google Scholar
• Rörth M. Effects of some organic phosphate compounds on the oxyhemoglobin dissociation curve in human erythrolysate. Scand. J. Clin. Lab. Invest. 1968; 22: 208
   PubMed Web of Science ®Google Scholar
• Bunn H. F., May M. H., Kocholaty W. F., Shields C. E. Hemoglobin function in stored blood. J. Clin. Invest. 1969; 48: 311
   PubMed Web of Science ®Google Scholar
• Huisman T. H. J., Boyd E. M., Kitchens J., Mayson S., Shepeard W. L. Oxygen equilibria and biochemical changes of whole blood stored in different preservation media. Transfusion 1969; 9: 180
   PubMedGoogle Scholar
• Valeri C. R., Hirsch N. M. Restoration in vivo of erythrocyte adenosine triphosphate, 2,3-diphosphoglycerate, potassium ion, and sodium ion concentrations following the transfusion of acid-citrate-dextrosestored human red blood cells. J. Lab. Clin. Med. 1969; 73: 722
   PubMed Web of Science ®Google Scholar
• Gabrio B. W., Donohue D. M., Huennekens F. M., Finch C. A. Erythrocyte preservation. VII. Acid-citrate-dextrose-inosine (ACDI) as a preservative for blood during storage at 4° C. J. Clin. Invest. 1956; 35: 657
   PubMed Web of Science ®Google Scholar
• Lenfant C., Torrance J., English E., Finch C. A., Reynafarje C., Ramos J., Faura J. Effect of altitude on oxygen binding by hemoglobin and on organic phosphate levels. J. Clin. Invest. 1968; 47: 2652
   PubMed Web of Science ®Google Scholar
• Eaton J. W., Brewer G. J., Grover R. F. Role of red cell 2,3-diphosphoglycerate in the adaption of man to altitude. J. Lab. Clin. Med. 1969; 73: 603
   PubMed Web of Science ®Google Scholar
• Valtis D. J., Kennedy A. C. Defective gas transport function of stored red blood cells. Lancet 1954; 266: 119
   PubMedGoogle Scholar