The Respiratory Function of the Blood

  • Giles F. Filley
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 6)


Study of the physiological mechanisms of oxygen transport makes particularly clear the distinction between the pressure of oxygen (or its chemical potential — an intensity factor) and the amount of oxygen (or, per unit volume, its concentration — a quantity factor). This distinction is more recognized in thermodynamics than in physiological chemistry; it is especially important in considering systems capable of dissociating (1,2,7).


Intensity Factor Oxygen Transport Dissociation Curve Carbon Dioxide Pressure 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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. (1).
    Clark, W.M.: The Determination of Hydrogen Ions. Baltimore, Williams and Wilkins Co., 3rd Ed., 1928, pp xiii, 35, 36.Google Scholar
  2. (2).
    Wyman, J., Jr.: Heme Proteins in Advances in Protein Chemistry. Ed. by M.L. Anson and J.T. Edsall, New York, Acad. Press, p 436, 1918.Google Scholar
  3. (3).
    Henderson, L.J.: Blood. A Study in General Physiology. New Haven, Yale Univ. Press, 1928.Google Scholar
  4. (4).
    Brewer, G.J., J.W. Eaton, J. Weil, and R.F. Grover: Red cell metabolism in health and disease: Studies of red cell glycolysis and interactions with carbon monoxide, smoking and altitude. This symposium.Google Scholar
  5. (5).
    Brody, J.S., and R.F. Coburn: Carbon monoxide-induced arterial hypoxemia. Science, 164, 1297, 1969.PubMedCrossRefGoogle Scholar
  6. (6).
    West, J.B.: Ventilation-perfusion inequality and overall gas exchange in computer models of the lung. Respiration Physiology, 7, 88, 1969.PubMedCrossRefGoogle Scholar
  7. (7).
    Wyman, J., Jr.: Linked functions and reciprocal effects in hemoglobin: A second look. Advances in Protein Chemistry, 19, 223, 1964.PubMedCrossRefGoogle Scholar
  8. (8).
    Rossi-Bernardi, L., and F.J.W. Roughton: The specific influence of carbon dioxide and carbamate compounds on the buffer power of hemoglobin and Bohr effects in human hemoglobin solutions. J. Physiol., 189, 1, 1967.PubMedGoogle Scholar
  9. (9).
    Perutz, M.F., H. Muirhead, L. Mazzarella, R.A. Crowther, J. Greer, and J.V. Kilmartin: Identification of residues responsible for the alkaline Bohr effect in hemoglobin. Nature, 222, 1240, 1969.PubMedCrossRefGoogle Scholar
  10. (10).
    Waddell, W.J., and R.G. Bates: Intracellular pH. Physiological Reviews, 49, 285, 1969.PubMedGoogle Scholar
  11. (11).
    Benesch, R., R.E. Benesch, and C.I. Yu. Reciprocal binding of oxygen and diphosphoglycerate. Proc. N.A.S., 59, 526, 1968.CrossRefGoogle Scholar
  12. (12).
    Roughton, F.J.W.: Handbook of Physiology, Sec. 3, Vol. I, p 814, American Physiol. Soc., Washington, D.C., 1964.Google Scholar

Copyright information

© Plenum Press, New York 1970

Authors and Affiliations

  • Giles F. Filley
    • 1
  1. 1.Webb-Waring Institute for Medical ResearchUniversity of Colorado Medical CenterDenverUSA

Personalised recommendations