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Diminution of the temperature effect on the oxygen affinity of hemoglobin after prolonged hypothermia

  • Heart, Circulation, Respiration and Blood; Environmental and Exercise Physiology
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Abstract

The influence of temperature on the oxygen affinity of hemoglobin, expressed as half saturation tension, P50, was investigated in male Sprague Dawley rats, which had been exposed to a cold environment for about 12 h. P50-values were determined by equilibrating blood samples to a knownP O 2 at different temperatures. The well known increase in oxygen affinity at low temperatures was observed, but after a longer hypothermic period this effect was diminished. This reduction of the temperature effect is manifested in a change of the ratio Δlog P50/ΔT from 0.022 in control experiments to 0.0115 in hypothermia. In cold adapted rats such an effect means a better oxygen supply to tissue at low body temperatures than in control animals. These changes in oxygen delivery after cold acclimatisation may partially be interpreted as the result of the decreased intraerythrocytic pH and elevated concentration of ATP found in the present study.

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Authors and Affiliations

  1. Institut für Physiologie der Universität Innsbruck, Fritz-Pregl-Strasse 3, A-6010, Innsbruck, Austria

    Heimo Mairbäurl

  2. Medizinische Klinik der Universität Innsbruck, Anichstrasse 35, A-6010, Innsbruck, Austria

    Egon Humpeler

Authors
  1. Heimo Mairbäurl
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  2. Egon Humpeler
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Mairbäurl, H., Humpeler, E. Diminution of the temperature effect on the oxygen affinity of hemoglobin after prolonged hypothermia. Pflugers Arch. 383, 209–213 (1980). https://doi.org/10.1007/BF00587520

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  • DOI: https://doi.org/10.1007/BF00587520

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