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The Contribution of Carbamate in Human Adult and Foetal Blood to the CO2 Exchange During the Respiratory Cycle

  • Christian Bauer
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 28)

Abstract

The reaction of carbon dioxide with the unprotonated form of amino groups yields carbamate and hydrogen ions according to the following reaction scheme:
$$R\, - \,NH_3^ + \, + \,\overset {K_z^1} \leftrightarrows \,R\, - \,N{H_2}\, + \,{H^ + }$$
$$ R\, - \,N{H_2}\, + \,C{O_2}\overset {K_c^1} \leftrightarrows \,R\, - \,NHCO{O^{ - \,}}\, + \,{H^ + }$$
At the hemoglobin molecule this reaction proceeds at the N-terminal amino groups of both α and β chins as it has been demonstrated by Kilmartin & Rossi-Bernardi (1969, 1971).

Keywords

Foetal Blood Oxygen Affinity Organic Phosphate Human Hemoglobin Bohr Effect 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bauer, C. (1969) Antagonistic influence of CO2 and 2, 3-diphosphoglycerate on the Bohr effect of human haemoglobin. Life Sci., 8: 1041.PubMedCrossRefGoogle Scholar
  2. Bauer, C. (1970) Reduction of the carbon dioxide affinity of human haemoglobin solutions by 2, 3 diphosphoglycerate., Resp. Physiol. 10: 10CrossRefGoogle Scholar
  3. Bauer, C. and Schroder, E. (1972) Carbamino compounds of haemoglobin in human adult and foetal blood. Submitted for publication.Google Scholar
  4. Benesch, R. and Benesch, R. E. (1967) The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Comm. 26: 162.PubMedCrossRefGoogle Scholar
  5. Benesch, R., Benesch, R. E. and Yu, C. I. (1968) Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Proc. Natl. Acad. Sci. ( U. S. ) 59: 526.CrossRefGoogle Scholar
  6. Benesch, R. E., Benesch, R., Bank, A., Renthal, R. and Bray, B. A. (1971) The preparation and properties of pyridoxylated hemoglobin. In:Genetical, Functional and Physical Studies of Hemoglobin. Karger, Basel.Google Scholar
  7. Bunn, H. F. and Briehl, R. F. (1970) The interaction of 2,3 diphosphoglycerate with various human hemoglobins. J. Clin. Invest. 49: 1088.PubMedCrossRefGoogle Scholar
  8. Chauntin, A. and Curnish, R. R. (1967) Effect of organic and and inorganic phosphates on the oxygen equilibrium of human erythrocytes. Arch. Biochem. Biophys. 121: 96.CrossRefGoogle Scholar
  9. Ferguson, J. K. W. (1936) Carbamino compounds of CO2 with human haemoglobin and their role in the transport of CO2. J. Physiol. ( Lond. ) 88: 40.Google Scholar
  10. Forster, R. E., Constantine, W. P., Craw, M. R., Rotman, H. H. and Klocke, R. A. (1968) Reaction of CO2 with human hemoglobin solution. J. biol. Chem. 243: 3317.PubMedGoogle Scholar
  11. Kernohan, J. C. Kreuzer, F., Rossi-Bernardi, L. and Roughton, F. J. W. (1966) The effects of bicarbonate and carbon dioxide on the affinity of haemoglobin for oxygen. Biochem. J. 100: 48PGoogle Scholar
  12. Kilmartin, J. V. and Rossi-Bernardi, L. (1969) Inhibition of CO2 combination and reduction of the Bohr effect in haemoglobin chemically modified at its α-amino groups. Nature 222: 1243PubMedCrossRefGoogle Scholar
  13. Kilmartin, J. V. and Rossi-Bernardi, L. (1971) The binding of carbon dioxide by horse haemoglobin. Biochem. J. 124: 31.PubMedGoogle Scholar
  14. Klocke, R. A. (1972) Influence of oxygenation, pH and 2, 3 diphosphoglycerat e on carbon dioxide exchange. Chest 61: 20SGoogle Scholar
  15. Pace. M., Rossi-Bernardi, L. and Roughton, F. J. W. (1970) The effect of organic phosphates on the reactions of haemoglobin and oxyhaemoglobin (carboxy-haemoglobin) with carbon dioxide. Biochem. J., 119: 67P.Google Scholar
  16. Perutz, M. F., Muirhead, H., Mazzarella, L., Crowther, R. A., Greer, J. and Kilmartin, J. V. (1969) Identification of residues responsible for the alkaline Bohr effect in haemoglobin. Nature 222: 1240PubMedCrossRefGoogle Scholar
  17. Renthal, R., Benesch, R. E., Benesch, R. and Bray. B. A. (1970) Affinity labelling of the polyphosphate binding site in hemoglobin with pyridoxal phosphate (PLP). Fed. Proc., 29: 732.Google Scholar
  18. Rossi-Bernardi, L. and Roughton, F. J. W. (1967) The specific influence of carbon dioxide and carbamate compounds on the buffer power and Bohr effect in human haemoglobin solutions. J. Physiol. ( Lond. ) 189: 1.Google Scholar
  19. Roughton, F. J. W. (1935) Recent work on carbon dioxide transport by the blood. Physiol. Rev. 15: 241.Google Scholar
  20. Roughton, F. J. W. (1970) Some recent work on the interactions of oxygen, carbon dioxide and haemoglobin. Biochem. J. 117: 801.PubMedGoogle Scholar
  21. Siggaard-Andersen, O. (1971) Oxygen linked hydrogen binding of human hemoglobin. Effects of carbon dioxide and 2, 3 diphosphoglycerate. Scand. J. Clin. Lab. Invest. 27: 351PubMedCrossRefGoogle Scholar
  22. Stadie, W. C. and O’Brien, H. (1937) The carbamate equilibrium II. The equilibrium of oxyhemoglobin and reduced hemoglobin. J. biol. Chem. 117: 439.Google Scholar
  23. Tomita, S. and Riggs, A. (1971) Studies on the interaction of 2, 3 diphosphoglycerate and carbon dioxide with hemoglobins from mouse, man and elephant. J. biol. Chem. 246: 547.PubMedGoogle Scholar
  24. Verdier, D. W. de and Garby, L. (1969) Low binding of 2, 3 diphosphoglycerate to haemoglobin F. Scand. J. Clin. Lab. Invest. 23: 149.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • Christian Bauer
    • 1
  1. 1.Physiologisches Institut der Medizinischen Hochschule3 HannoverW. Germany

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