Literature DB >> 6413092

An equilibrium model of the oxygen association curve of normal human erythrocytes under standardized conditions.

R G Ryall, C J Story.   

Abstract

Hemoglobin-oxygen association curves of human erythrocytes were measured in metabolically stable cells under the standardized conditions of extracellular pH 7.400, carbon dioxide tension 38 mmHg (approximately 5 kPa) and temperature 37 degrees C. A model of the oxygen association curve of normal erythrocytes was subsequently developed, based on assumed equilibrium reactions between hemoglobins (Hb), oxygen, and 2,3-diphosphoglycerate (DPG). Conditional equilibrium constants were determined for reactions leading to the formation of species designated Hb-O2 (K = 0.14 mmHg-1), Hb-(O2)4 (K = 0.44 X 10(-4) mmHg-4), Hb-DPG (K = 0.30 X 10(4) L mol-1) and Hb-O2-DPG (K = 0.61 X 10(2) L mol-1 mmHg-1) for unmodified hemoglobin, and Hb-O2 (K = 0.14 mmHg-1) and Hb-(O2)4 (K = 0.44 X 10(-4) mmHg-4) for glycosylated hemoglobin. This model provides a practical means of calculating the expected oxygen association curve for a sample of erythrocytes under standardized conditions, given the intracellular concentrations of hemoglobins and 2,3-diphosphoglycerate and the assumption that the hemoglobins in those cells function normally.

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Year:  1983        PMID: 6413092

Source DB:  PubMed          Journal:  Clin Chem        ISSN: 0009-9147            Impact factor:   8.327


  2 in total

1.  Involvement of oxidative damage in erythrocyte lysis induced by amphotericin B.

Authors:  J Brajtburg; S Elberg; D R Schwartz; A Vertut-Croquin; D Schlessinger; G S Kobayashi; G Medoff
Journal:  Antimicrob Agents Chemother       Date:  1985-02       Impact factor: 5.191

2.  Erythrocyte 2,3-bisphosphoglycerate concentrations and haemoglobin glycosylation in normoxic Type 1 (insulin-dependent) diabetes mellitus.

Authors:  A P Roberts; C J Story; R G Ryall
Journal:  Diabetologia       Date:  1984-05       Impact factor: 10.122

  2 in total

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