19
Views
17
CrossRef citations to date
0
Altmetric
Original Article

Oxygen-Linked Hydrogen Ion Binding of Human Hemoglobin. Effects of Carbon Dioxide and 2,3-Diphosphoglycerate: IV. Thermodynamical Relationship between the Variables

, , , &
Pages 303-320 | Received 30 Sep 1971, Accepted 10 Nov 1971, Published online: 08 Jul 2009

References

  • Adair G. S. Thermodynamical proof of the reciprocal relationship of oxygen and carbon dioxide in blood. J. Physiol. (Lond.) 1923; 58: IV–V
  • Antonini E. Oxygen binding to hemoglobin. Influence of solvent components. Symposium on Intracellular Regulation of Hemoglobin Affinity to Oxygen. Swedish J. Defence Medicine 1969; 5: 147, 147–153, in deVerdier, C.-H., Garby, L., Högman, C. F. & Åkerblom, O. (eds.)
  • Antonini E. The effect of anions on the O2 equilibrium of hemoglobin. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 121–130
  • Bartels H. The biological significance of the Bohr effect. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 717–735
  • Bauer Ch. Antagonistic influence of CO2 and 2,3-diphosphoglycerate on the Bohr effect of human haemoglobin. Life Sci. 1969; 8: 1041
  • Bauer Ch. Reduction of the carbon dioxide affinity of human hemoglobin solutions by 2,3-diphosphoglycerate. Resp. Physiol. 1970; 10: 10
  • Bauer Ch. The role of organic phosphates in the gas transport of maternal and foetal blood. Gas Exchange Across the Placenta. U. S. Government Printing Office, 000–000, In press
  • Benesch R., Benesch, Ruth E. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. biophys. Res. Commun. 1967; 26: 162
  • Benesch R., Benesch, Ruth E., Yu C. I. Reciprocal binding of oxygen and diphospho-glycerate by human hemoglobin. Proc. nat. Acad. Sci. (Wash.) 1968; 59: 526
  • Bohr C., Hasselbalch K., Krogh A. S. Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt. Skand. Arch. Physiol. 1904; 16: 402
  • Chanutin A., Curnish R. R. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes. Arch. Biochem. 1967; 121: 96
  • Christiansen, Johanne, Douglas C. G., Haldane J. S. The absorption and dissociation of carbon dioxide by human blood. J. Physiol. (Lond.) 1914; 48: 244
  • Edsall J. T., Wyman J. Biophysical Chemistry. Vol. I. Thermodynamics, Electrostatics, and the Biological Significance of the Properties of Matter. Academic Press, New York 1958
  • Garby L., Gerber G., de Verdier C.-H. Binding of ATP and 2,3-DPG to hemoglobin. Stoffwechsel und Membranpermeabilität von Erythrocyten und Thrombocyten, E. Deutsch, E. Gerlach, K. Moser. G. Thieme, Stuttgart 1968; 66–69
  • Garby L., Gerber G., de Verdier C.-H. Binding of 2,3-diphosphoglycerate and adenosine triphosphate to human hemoglobin A. Europ. J. Biochem. 1969; 10: 110
  • Garby L., deVerdier C.-H. Affinity of human hemoglobin A to 2,3-diphosphoglycerate. Effect of hemoglobin concentration and of pH. Scand. J. clin. Lab. Invest. 1971; 27: 345
  • Garby L., DeVerdier C.-H. Binding of 2,3-diphosphoglycerate to human hemoglobin A. Effects of pH, hemoglobin concentration and carbon dioxide. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 236–242
  • Garby L., Robert M., Zaar B. Proton- and carbamino-linked oxygen affinity of normal human blood. Acta physiol. scand., In press
  • Haar ter D., Wergeland H. Elements of Thermodynamics. Addison-Wesley, Palo Alto 1966
  • d'A. Heck H. A general derivation of the binding potential (letter to the edior). J. mol. Biol. 1970; 50: 703
  • Hill A. V. The possible effects of aggregation of molecules of hemoglobin and its dissociation curve. J. Physiol. (Lond.) 1910; 40: IV–VII
  • Hilpert P., Fleischmann, Renate G., Kempe, Doris, Bartels H. The Bohr effect related to blood and erythrocyte pH. Amer. J. Physiol. 1963; 205: 337
  • Kernohan J. C., Forster R. E. II. pH. dependence of oxyhemoglobin dissociation at high oxygen tension: a revaluation. J. appl. Physiol. 1967; 23: 802
  • Margaria R. The contribution of hemoglobin to acid-base equilibrium of the blood in health and disease. Clin. Chem. 1957; 3: 306
  • Näraa 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
  • Näraa 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
  • 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 (Lond.) 1970; 228: 726
  • Rörth M., Nygaard S. Estimation of 2,3-DPG in whole blood. Swedish J. Defence Medicine 1969; 5: 177
  • Rörth M. Dependence of oxyhemoglobin dissociation and intraerythrocytic 2,3-DPG on acid-base status of blood. I. In vitro studies on reduced and oxygenated blood. Red Cell Metabolism and Function, G. J. Brewer. Plenum Press, New York 1970; 57–65
  • Rörth M. Review of hemoglobin interactions and red cell metabolism. Series Haematolog., in press
  • Rooth G., Caligara F. The influence of metabolic acid-base variation on the oxygen dissociation curve. Clin. Sci. 1961; 21: 393
  • Rossi-Bernardi L., Pace M., Roughton F. J. W., Van Kempen L. The estimation of hemoglobin-CO2 compounds by gel filtration and ion-exchange chromatography. CO2: Chemical, Biochemical, and Physiological Aspects, R. E. Forster, J. T. Edsall, A. B. Otis, F. J. W. Roughton, Washington 1969; 65–71, NASA SP-188
  • 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
  • Rossi-Bernardi L., Roughton F. J. W., Pace M., Coven E. The effects of organic phosphates on the binding of CO2 to human haemoglobin and on CO2 transport in the circulating blood. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 220–235
  • Roughton F. J. W. Some recent work on the interactions of oxygen, carbon dioxide and haemoglobin. Biochem. J. 1970; 117: 801
  • Severinghaus J. W. Blood gas calculator. J. appl. Physiol. 1966; 21: 1108
  • Siggaard-Andersen O. The first dissociation exponent of carbonic acid as a function of pH. Scand. J. clin. Lab. Invest. 1962; 14: 587
  • Siggaard-Andersen O. Oxygen-linked hydrogen ion binding of human hemoglobin. Effects of carbon dioxide and 2,3-diphosphoglycerate. I. Studies on erythrolysate. Scand. J. clin. Lab. Invest. 1971; 27: 351
  • Siggaard-Andersen O. Comparison of the Bohr effect and the Haldane effect. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 166–174
  • 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: 361
  • Siggaard-Andersen O., Salling N., Nörgaard-Pedersen B., Rörth M. Oxygen-linked hydrogen ion binding of human hemoglobin. Effects of carbon dioxide and 2,3-diphosphoglycerate. III. Comparison of the Bohr effect and the Haldane effect. Scand. J. clin. Lab. Invest. 1972; 29: 185
  • Tomita S., Riggs A. Studies of the interaction of 2,3-diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man, and elephant. J. biol. Chem. 1971; 246: 574
  • Tyuma I., Imai K., Shimizu K. Organic phosphates and the oxygen equilibrium function of some human hemoglobins. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 131–161
  • Wyman J. Heme proteins. Advanc. Protein Chem. 1948; 4: 407
  • Wyman J. Linked functions and reciprocal effects in hemoglobin. A. second look. Advanc. Protein Chem. 1964; 19: 223
  • Wyman J. The binding potential. A neglected linkage concept. J. mol. Biol. 1965; 11: 631
  • Wyman J. Allosteric linkage. J. Amer. Chem. Soc. 1967; 89: 2202
  • Wyman I. Regulation in macromolecules as illustrated by hemoglobin. Quart. Rev. Biophys. 1968; 1: 35
  • Wyman J. Reflections regarding hemoglobin. Oxygen Affinity of Hemoglobin and Red Cell Acid-Base Status. Alfred Benzon Symposium IV, M. Rörth. Munksgaard, Copenhagen 1972; 37–53

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.