Oxygen-Linked Hydrogen Ion Binding of Human Hemoglobin. Effects of Carbon Dioxide and 2,3-Diphosphoglycerate I. Studies on Erythrolysate

References

• Antonini E., Wyman J., Brunori M., Fronticelli C., Bucci E., Rossi-Fanelli A. Studies on the relations between molecular and functional properties of hemoglobin V. The influence of temperature on the Bohr effect in human and in horse hemoglobin. J. biol. Chem. 1965; 240: 1096
   PubMed Web of Science ®Google Scholar
• Bauer Ch. Antagonistic influence of CO2 and 2,3 diphosphoglycerate on the Bohr effect of human haemoglobin. Life Sci. 1969; 8: 1041
   PubMed Web of Science ®Google Scholar
• Bauer Ch. Reduction of the carbon dioxide affinity of human hemoglobin solutions by 2,3 diphosphoglycerate. Resp. Physiol. 1970; 10: 10
   PubMedGoogle Scholar
• Benesch R., Benesch, Ruth E., Enoki Y. The interaction of hemoglobin and its subunits with 2,3-diphosphoglycerate. Proc. nat. Acad. Sci. (Wash.) 1968; 61: 1102
   PubMedGoogle Scholar
• Benesch, Ruth 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
• Bohr C., Hasselbalch K., Krogh A. S. Ueber einen in biologischer Beziehung wich-tigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt. Scand. Arch. Physiol. 1904; 16: 402
   Google Scholar
• Christiansen, Johanne, Douglas C. G., Haldane J. S. The absorption and dissociation of carbon dioxide by human blood. J. Physiol. (Lond.) 1914; 48: 244
   Google Scholar
• Garby L., Gerber G., deVerdier C.-H. Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human hemoglobin A. Europ. J. Biochem. 1969; 10: 110
   PubMedGoogle Scholar
• German B., Wyman J., Jr. The titration curves of oxygenated and reduced hemoglobin. J. biol. Chem. 1937; 117: 533
   Google Scholar
• Hastings A. B., Van Slyke D. D., Neill J. M., Heidelberger M., Harington C. R. Studies of gas and electrolyte equilibria in blood. IV. The acid properties of reduced and oxygenated hemoglobin. J. biol. Chem. 1924; 60: 89
   Google Scholar
• Henriques O. M. Über Carbhämoglobin. Ergebn. Physiol. 1929; 28: 625
   Google Scholar
• Kernohan J. C., Forster R. E., II. pH dependence of oxyhemoglobin dissociation at high oxygen tension: a revaluation. J. appl. Physiol. 1967; 23: 802
   PubMed Web of Science ®Google Scholar
• Kilmartin J. V., Rossi-Bernardi L. Inhibition of CO2 combination and reduction of the Bohr effect in haemoglobin chemically modified at its α-amino groups. Nature 1959; 222: 1243
   Google Scholar
• Kilmartin J. V., Wootton J. Inhibition of Bohr effect after removal of C-terminal histidines from haemoglobin β-chains. Nature 1970; 228: 766
   PubMed Web of Science ®Google Scholar
• Margaria R., Green A. A. The first dissociation constant. pK1, of carbonic acid in hemoglobin solutions and its relation to the existence of a combination of hemoglobin with carbon dioxide. J. biol. Chem. 1933; 102: 611
   Google Scholar
• Næraa N., Petersen E. S., Boye E. The influence of simultaneous, independent changes in pH and carbon dioxide tension on the in vitro oxygen tension-saturation relationship of human blood. Scand. J. clin. Lab. Invest. 1963; 15: 141
   PubMed Web of Science ®Google Scholar
• Næraa N., Petersen E. S., Boye E., Severinghaus J. W. pH and molecular CO2 components of the Bohr effect in human blood. Scand. J. clin. Lab. Invest. 1966; 18: 96
   PubMed Web of Science ®Google Scholar
• Pace M., Rossi-Bernardi L., Roughton F. J. W. The effect of organic phosphates on the reactions of haemoglobin and oxyhaemoglobin (carboxyhaemoglobin) with carbon dioxide. Biochem. J. 1970; 119: 67
   PubMedGoogle Scholar
• Perutz M. F. Structure and function of haemoglobin. I. A tentative atomic model of horse oxyhaemoglobin. J. molec. Biol. 1965; 13: 646
   Web of Science ®Google Scholar
• Perutz M. F., Muirhead H., Mazzarella L., Crowther R. A., Greer J., Kilmartin J. V. Identification of residues responsible for the alkaline Bohr effect in haemoglobin. Nature 1969; 222: 1240
   PubMed Web of Science ®Google Scholar
• Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Haem-haem interaction and the problem of allostery. The Bohr effect and combination with organic phosphates. Nature 1970; 228: 726
   PubMed Web of Science ®Google Scholar
• Richterich R. Klinische Chemie, Theorie und Praxis. Akad. Verlagsges. 1968, Frankfurt a. M., 2. erw. Aufl.
   Google Scholar
• Rörth M., Nygaard S. Estimation of 2,3-DPG in whole blood. Försvarsmedicin 1969; 5: 177
   Google Scholar
• Rörth M. Method for increasing the DPG concentration of erythrocytes, Personal communication
   Google Scholar
• Rossi-Bernardi L., Roughton F. J. W. The specific influence of carbon dioxide and carbamate compounds on the buffer power and Bohr effects in human hemoglobin solutions. J. Physiol. (Lond.) 1967; 189: 1
   Google Scholar
• Roughton F. J. W. Some recent work on the interactions of oxygen, carbon dioxide and haemoglobin. Biochem. J. 1970; 117: 801
   PubMed Web of Science ®Google Scholar
• Salling N., Siggaard-Andersen O. Liquid-junction potentials between plasma or erythro-lysate and KC1 solutions. Scand. J. clin. Lab. Invest
   Google Scholar
• Severinghaus J. W. Blood gas calculator. J. appl. Physiol. 1966; 21: 1108
   PubMed Web of Science ®Google Scholar
• Siggaard-Andersen O. The first dissociation exponent of carbonic acid as a function of pH. Scand. J. clin. Lab. Invest. 1962; 14: 587
   PubMed Web of Science ®Google Scholar
• Siggaard-Andersen O., Engel K., Jörgensen K., Astrup P. A micro method for determination of pH, carbon dioxide tension, base excess, and standard bicarbonate in capillary blood. Scand. J. clin. Lab. Invest. 1960; 12: 172
   PubMed Web of Science ®Google Scholar
• Siggaard-Andersen O., Jörgensen K., Næraa N. Spectrophotometric determination of oxygen saturation in capillary blood. Scand. J. clin. Lab. Invest. 1962; 14: 298
   PubMed Web of Science ®Google Scholar
• Siggaard-Andersen O., Salling N. Oxygen-linked hydrogen ion binding of human hemoglobin. Effects of carbon dioxide and 2,3-diphosphoglycerate. II. Studies on whole blood. Scand. J. clin. Lab. Invest. 1971; 27
   Google Scholar
• Wyman J. Heme proteins. Advanc. Protein Chem. 1948; 4: 407
   PubMedGoogle Scholar
• Wyman J. Linked functions and reciprocal effects in hemoglobin. A second look. Advanc. Protein Chem. 1964; 19: 223
   PubMedGoogle Scholar