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Oxygen Transport to Tissue VII pp 63–73Cite as

Blood Gas Transport and 2,3-DPG

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 191))

Abstract

Since the discovery of the sensitivity of oxygen-hemoglobin interaction to the concentration of red cell 2,3-diphosphoglycerate (Benesch and Benesch, 1967; Chanutin and Curnish, 1967), a great number of investigators have explored its biochemical, physiological and clinical ramifications. The following is a brief overview of this work, with particular emphasis upon the role of DPG in blood oxygen transport in health and disease.

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References

  • Apstein, C. S., Dennis, R. C., Briggs, L., Vogel, W. M., Frazer, J., and Valeri, C. R., 1984, Effect of red blood cell storage on cardiac performance: Improved myocardial oxygen delivery and function during constant flow coronary perfusion with low oxy-hemoglobin affinity human red blood cells in normothermic and hypothermic rabbit hearts, Office of Naval Research, Contract N0014–79-C-0168, Technical Report No. 83–01.

    Google Scholar 

  • Arturson, G., Garby, L., Robert, M. and Zaar, B., 1974, The O2 dissociation curve of normal human blood with special reference to the influence of physiological effector ligands, Scand. J. clin. Lab. Invest., 34:9.

    Article  PubMed  CAS  Google Scholar 

  • Astrup, P., Rørth, M., and Thorshauge, C., 1970, Dependency on acid-base status of oxyhemoglobin dissociation and 2,3-diphosphoglycerate level in human erythrocytes. II. In vivo studies, Scand. J. clin. Lab. Invest., 26:47.

    Article  PubMed  CAS  Google Scholar 

  • Baldwin, J. M., 1975, Structure and function of hemoglobin, Prog. Biophys. Molec. Biol., 29:225.

    CAS  Google Scholar 

  • Bauer, C., 1970, Reduction of the carbon dioxide affinity of human hemoglobin solutions by 2,3-diphosphoglycerate, Resp. Physiol., 10:10.

    Article  CAS  Google Scholar 

  • Bauer, C., Klocke, R. A., Kamp, D., and Forster, R. E., 1973, Effect of 2,3-diphosphoglycerate and H+ on the reaction of O2 and hemoglobin, Am. J. Physiol., 224:838.

    PubMed  CAS  Google Scholar 

  • Benesch, R. and Benesch, R. E., 1967, The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin, Biochem. Biophys. Res. Commun., 26:162.

    Article  PubMed  CAS  Google Scholar 

  • Chanutin, A. and Curnish, P., 1967, Effect of organic and inorganic phosphate on the oxygen equilibrium of human erythrocytes, Arch. Biochem. Biophys., 121:96.

    Article  PubMed  CAS  Google Scholar 

  • Deuticke, B., Duhm, J., and Dierkesmann, R.,1971, Maximal elevation of 2,3-diphosphoglycerate concentrations in human erythrocytes: Influence on glycolytic metabolism and intracellular pH, Pflugers Arch., 326:15.

    Article  PubMed  CAS  Google Scholar 

  • Duhm, J., 1971, Effects of 2,3-diphosphoglycerate and other organic phosphate compounds on oxygen affinity and intracellular pH of human erythrocytes, Pflugers Arch., 326:341.

    Article  PubMed  CAS  Google Scholar 

  • Duhm, J., 1976, Influence of 2,3-diphosphoglycerate on the buffering properties of human blood. Role of the red cell membrane, Pflugers Arch., 363:61.

    Article  PubMed  CAS  Google Scholar 

  • Duhm, J. and Gerlach, E.,1971, On the mechanism of the hypoxia-induced increase of 2,3-diphosphoglycerate in erythrocytes, Pflugers Arch., 326:254.

    Article  PubMed  CAS  Google Scholar 

  • Ellis, C. G., Potter, R. F., and Groom, A.C.,1983, The Krogh cylinder is not appropriate for modelling O2 transport in contracted skeletal muscle, Adv. Exper. Med. Biol., 159:253.

    Article  CAS  Google Scholar 

  • Harken, A. H., 1977, The surgical significance of the oxyhemoglobin dissociation curve, Surg. Gynec. Obstet., 144:935.

    PubMed  CAS  Google Scholar 

  • Hlastala, M. P. and Woodson, R. C., 1983, Bohr effect data for blood gas calculations, J. Appl. Physiol., 55:1002.

    PubMed  CAS  Google Scholar 

  • Honig, C. R., Gayeski, R. E. J. Federspiel, W., Clark, A. Jr., and Clark, P., 1984, Muscle O2 gradients from hemoglobin to cytochrome: new concepts, new complexities, Adv. Exper. Med. Biol., 169:23.

    Article  CAS  Google Scholar 

  • Kilmartin, J.V. and Rossi-Bernardi, L., 1973, Interaction of hemoglobin with hydrogen ions, carbon dioxide and organic phosphates, Physiol. Rev., 53:836.

    PubMed  CAS  Google Scholar 

  • Lichtman, M. A., Murphy, M. S., Whitbeck, A. A., and Kearney, E, A., 1974, Oxygen binding to haemoglobin in subjects with hypoproliferative anaemia, with and without chronic renal disease: Role of pH, Brit. J. Haemat., 27:439.

    Article  PubMed  CAS  Google Scholar 

  • Minakami, S. and Yoshikawa, H., 1966, Studies on erythrocyte glycolysis. III. The effects of active cation transport, pH and inorganic phosphate concentration on erythrocyte glycolysis, J. Biochem. (Tokyo), 59:145.

    CAS  Google Scholar 

  • Nylander, E., Lund, N. and Wranne, B., 1983, Effect of increased blood oxygen affinity on skeletal muscle surface oxygen pressure fields, J. Appl. Physiol., 54:99.

    PubMed  CAS  Google Scholar 

  • Ross, B. K. and Hlastala, M. P., 1981, Increased hemoglobin-oxygen affinity does not decrease skeletal muscle oxygen consumption, J. Appl. Physiol., 51:864.

    PubMed  CAS  Google Scholar 

  • Salhany, J. M., Eliot, R. S., and Mizukami, H., 1970, The effect of 2,3-diphosphoglycerate on the kinetics of deoxygenation of human hemoglobin, Biochem. Biophys. Res. Commun., 39:1052.

    Article  PubMed  CAS  Google Scholar 

  • Samaja, M., Mosca, A., Luzzana, M., Rossi-Bernardi, L., and Winslow, R., 1981, Equations and nomogram for the relationship of human blood p50 to 2,3-diphosphoglycerate, CO2 and H+, Clin. Chem., 27:1856.

    PubMed  CAS  Google Scholar 

  • Samaja, M. and Winslow, R., 1979, The separate effects of H+ and 2,3-DPG on the oxygen equilibrium curve of human blood, Brit. J. Haemat., 41:373.

    Article  PubMed  CAS  Google Scholar 

  • Siggaard-Andersen, O.., 1974, “The Acid-Base Status of the Blood,” Munskgaard, Copenhagen.

    Google Scholar 

  • Soulard, C. D., Teisscire, B. P., TeisScire, L. J., and Herigault, R. A., 1983, Consequences of an acute increase in p50 in anaesthetized guinea pigs, Respir. Physiol., 51:21.

    Article  PubMed  CAS  Google Scholar 

  • Valeri, C. R., 1984, Clinical importance of the oxygen transport function of preserved red blood cells, in: “Proc. 12th Katzir-Katchalsky meeting on oxygen transport by red blood cells”, Pergamon, Oxford, in press.

    Google Scholar 

  • Valeri, C. R. and Hirsch, N. M., 1969, Restoration in vivo of erythrocyte adenosine triphosphate, 2,3-diphosphoglycerate, potassium ion and sodium ion concentration following transfusion of acid-citrate-dextrose-stored human red blood cells, J. Lab. Clin. Med., 73:722.

    PubMed  CAS  Google Scholar 

  • Winslow, R. M., Samaja, M., Winslow, N. J«, Rossi-Bernardi, L., and Shrager, R. I., 1983, Simulation of continuous blood O2 equilibrium curve over physiological pH, DPG and pC02 range, J. Appl. Physiol., 54:524.

    Article  PubMed  CAS  Google Scholar 

  • Woodson, R. D. and Auerbach, S., 1982, Effect of increased oxygen affinity and anemia on cardiac output and its distribution, J. Appl. Physiol., 53:1299.

    PubMed  CAS  Google Scholar 

  • Woodson, R. D., Fitzpatrick, J. H. Jr., Costello, D. J., and Gilboe, D. D., 1982, Increased brain oxygen affinity decreases canine brain oxygen consumption, J. Lab. Clin. Med., 100:411.

    PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Chemical Engineering Department, Tufts University, Medford, Mass., 02155, USA

    Jerry H. Meldon

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  1. Jerry H. Meldon
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Editor information

Editors and Affiliations

  1. University of Nijmegen, Nijmegen, The Netherlands

    F. Kreuzer  & Z. Turek  & 

  2. University of Alabama at Birmingham, Birmingham, Alabama, USA

    S. M. Cain

  3. Northwestern University, Evanston, Illinois, USA

    T. K. Goldstick

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© 1985 Plenum Press, New York

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Meldon, J.H. (1985). Blood Gas Transport and 2,3-DPG. In: Kreuzer, F., Cain, S.M., Turek, Z., Goldstick, T.K. (eds) Oxygen Transport to Tissue VII. Advances in Experimental Medicine and Biology, vol 191. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3291-6_5

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  • DOI: https://doi.org/10.1007/978-1-4684-3291-6_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3293-0

  • Online ISBN: 978-1-4684-3291-6

  • eBook Packages: Springer Book Archive

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