Literature DB >> 6776481

Temperature and oxygenation of human blood at constant total CO2 content.

M Castaing, M Sinet.   

Abstract

The influence of temperature on the oxygeneration of normal and 2,3-diphosphoglycerate-depleted human blood suspensions (final hemoglobin concentration: 0.75%) was studied under closed-system conditions (constant total CO2 content) beginning with standard values:pH 7.40, Pco2 40 torr, at 37 degrees C. The present results quantify the temperature-induced changes in Po2 occuring in association with the concomitant acid-base variations prevailing in a closed system. When the temperature was raised from 25 to 42 degrees C, P50 varied from 13.9 +/- 1.1 to 40.7 +/- 1.9 torr in the presence of 2,3-DPG and from 7.6 +/- 0.4 to 24.8 +/- 1.2 torr in the absence of the cofactor. The derived equations correlate Po2 variations with those of temperature (T: 25--42 degrees C) and oxygen saturation (So2:10--90%). The temperature coefficient of oxygenation and the DPG-induced decrease in the heat of hemoglobin oxygenation were shown to be saturation dependent. DPG lowered dlog Po2/dT from 0.0299 to 0.0275 and delta H from --12.9 to --11.8 kcal/mole O2 bound at 50% So2 but had no significant influence on these parameters for So2 less than or equal to 20%. The results suggest that the release of carbamate at the beginning of oxygenation is virtually unaffected by presence of 2,3-DPG in the 25--42 degree C temperature range.

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Year:  1980        PMID: 6776481     DOI: 10.1007/bf00584200

Source DB:  PubMed          Journal:  Pflugers Arch        ISSN: 0031-6768            Impact factor:   3.657


  19 in total

1.  Temperature-induced changes in blood acid-base status: pH and PCO2 in a binary buffer.

Authors:  R B Reeves
Journal:  J Appl Physiol       Date:  1976-05       Impact factor: 3.531

2.  Hydrogen ion regulation, temperature, and evolution.

Authors:  H Rahn; R B Reeves; B J Howell
Journal:  Am Rev Respir Dis       Date:  1975-08

3.  Influence of temperature on hemoglobin-ligand interaction in whole blood.

Authors:  M P Hlastala; R D Woodson; B Wranne
Journal:  J Appl Physiol Respir Environ Exerc Physiol       Date:  1977-09

4.  Effect of 2, 3-diphosphoglycerate on the oxygen affinity and on the proton- and carbamino-linked oxygen affinity of hemoglobin in human whole blood.

Authors:  G Arturson; L Garby; B Wranne; B Zaar
Journal:  Acta Physiol Scand       Date:  1974-11

5.  Proton- and carbamino-linked oxygen affinity of normal human blood.

Authors:  L Garby; M Robert; B Zaar
Journal:  Acta Physiol Scand       Date:  1972-04

6.  Stereochemistry of cooperative effects in haemoglobin.

Authors:  M F Perutz
Journal:  Nature       Date:  1970-11-21       Impact factor: 49.962

7.  The oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration.

Authors:  R E Benesch; R Benesch; C I Yu
Journal:  Biochemistry       Date:  1969-06       Impact factor: 3.162

8.  The influence of temperature and pH on the dissociation curve of oxyhemoglobin of human blood.

Authors:  P Astrup; K Engel; J W Severinghaus; E Munson
Journal:  Scand J Clin Lab Invest       Date:  1965       Impact factor: 1.713

9.  Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin.

Authors:  R Benesch; R E Benesch; C I Yu
Journal:  Proc Natl Acad Sci U S A       Date:  1968-02       Impact factor: 11.205

10.  Temperature and acid-base status of human blood at constant and variable total CO2 content.

Authors:  M Castaing; J J Pocidalo
Journal:  Respir Physiol       Date:  1979-10
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