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Oxygen Binding of Modified Hemoglobins in Solution

  • D. Mauldin
  • R. L. Dalpé
  • P. J. Anderson
  • G. P. Biro
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 248)

Abstract

The need for an oxygen-carrying blood substitute has been recognized for many years, and while various solutions and fluorocarbons have been tried, these have not met with the desired success. Though hemoglobin itself would seem a natural choice for this task, several undesirable properties must be overcome to render it suitable for large volume replacement applications. Hemoglobin, in concentrations appropriate for sufficient oxygen delivery to tissues, exhibits an undesirably high oncotic pressure, and is rapidly eliminated from the circulation. Additionally, in human red blood cells, the oxygen affinity of hemoglobin is partially regulated by 2,3-bisphosphoglycerate (BPG), (P50 = 24–30mm Hg), whereas hemoglobin, free in solution and devoid of BPG, has a much higher affinity for oxygen (P50 =12–16mm Hg) ; its ability to unload oxygen to tissues thus is substantially impaired.

Keywords

Sodium Borohydride Hill Slope Oxygen Affinity Blood Substitute Hemoglobin Solution 
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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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • D. Mauldin
    • 1
  • R. L. Dalpé
    • 1
  • P. J. Anderson
    • 1
  • G. P. Biro
    • 1
  1. 1.Departments of Physiology and BiochemistryUniversity of OttawaCanada

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