Response of erythrocytic 2,3-diphosphoglycerate to strenuous exercise

  • J. M. Ramsey
  • S. William PipolyJr.


Since increases of erythrocytic 2,3-diphosphoglycerate (2,3-DPG) have been shown to enhance the release of oxygen from hemoglobin, experiments were designed to evaluate the response of 2,3-DPG to two different workloads in 13 fasted human subjects. No significant mean change in 2,3-DPG was found following 16 min of strenuous exercise on a bicycle ergometer, but when the subjects were subjected later to a greater workload for 20 min, there was a significant mean decrease in 2,3-DPG despite much individual variation. In addition, there was a significant positive correlation of 2,3-DPG reduction with increases in postexercise lactate, and a significant inverse correlation of oxygen consumption during exercise with postexercise lactate. The data suggest that the 2,3-DPG mechanism may not be compensating in exercise when the workload requires a preponderance of anaerobic metabolism promoting lactacidaemia.

Key words

2,3-DPG Exercise Hypoxia 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Austin, P. L., Stegink, L. D., Gisolfi, C. V., Lauer, R. M.: The effect of exercise on red blood cell 2,3-diphosphoglycerate in children. J. Pediatr. 83, 41–45 (1973)Google Scholar
  2. Bellingham, A. J., Detter, J. C., Lenfant, C.: Regulatory mechanisms of hemoglobin oxygen affinity in acidosis and alkalosis. J. Clin. Invest. 50, 700–706 (1971)Google Scholar
  3. Benesch, R., Benesch, R. E.: The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin. Biochem. Biophys. Res. Kommun. 26, 162–167 (1967)Google Scholar
  4. Benesch, R., Benesch, R. E., Yu, C. I.: Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin. Biochemistry 59, 526–532 (1968)Google Scholar
  5. Böning, D., Schweigart, U., Tibes, U., Hemmer, B.: Influence of exercise and endurance training on the oxygen dissociation curve of blood under in vivo and in vitro conditions. Eur. J. Appl. Physiol. 34, 1–10 (1975)Google Scholar
  6. Chanutin, A., Curnish, R. R.: Effect of organic and inorganic phosphate on the oxygen equilibrium of human erythrocytes. Arch. Biochem. Biophys. 121, 96–102 (1967)Google Scholar
  7. Dempsey, J. A., Rodriquez, J., Shahidi, N. T., Reddan, W. G., MacDougall, J. D.: Muscular exercise, 2,3-DPG and oxy-hemoglobin affinity. Int. Z. Angew. Physiol. 30, 34–39 (1971)Google Scholar
  8. Eaton, J. W., Brewer, G. J.: The relationship between red cell 2,3-diphosphoglycerate and levels of hemoglobin in the human. Biochemistry 61, 756–760 (1968)Google Scholar
  9. Eaton, J. W., Faulkner, J. A., Brewer, G. J.: Response of the human red cell to muscular activity. Proc. Soc. Exp. Biol. Med. 132, 886–887 (1969)Google Scholar
  10. Edwards, M. J., Cannon, B.: Oxygen transport during erythropoietic response to moderate blood loss. N. Engl. J. Med. 287, 115–118 (1972)Google Scholar
  11. Friedemann, T. E., Hauger, G. E.: Collection of blood for the determination of pyruvic and lactic acids. J. Biol. Chem. 144, 67–77 (1942)Google Scholar
  12. Ramsey, J. M., Casper, P. W.: Effect of carbon monoxide exposures on erythrocytic 2,3-DPG in rabbits. J. Appl. Physiol. 41, 689–692 (1976)Google Scholar
  13. Ramsey, J. M., Korchmaros, B. Z.: Effect of oxygen desaturation from carbon monoxide inhalation on erythrocytic 2,3-DPG. Ohio Jour. Sci. (In press, 1978)Google Scholar
  14. Remes, K., Harkonen, M., Vuopio, P., Peltokallio, P.: The decrease in red cell 2,3-diphosphoglycerate concentration in long distance running. J. Sports Med. 15, 113–116 (1975)Google Scholar
  15. Rose, Z. B.: Enzyme controlling 2,3-diphosphoglycerate in human erythrocytes. Fed. Proc. 29, 1105–1111 (1970)Google Scholar
  16. Rose, Z. B., Liebowitz, J.: Direct determination of 2,3-diphosphoglycerate. Anal. Biochem. 35, 177–180 (1970)Google Scholar
  17. Shappell, S. D., Murray, J. A., Bellingham, A. J., Woodson, R. D., Detter, J. C., Lenfant, C.: Adaptation to exercise: role of hemoglobin affinity for oxygen and 2,3-diphosphoglycerate. J. Appl. Physiol. 30, 827–832 (1971)Google Scholar
  18. Taunton, J. E., Taunton, C. A., Banister, E. W.: Alterations in 2,3-dpg and P50 with maximal and submaximal exercise. Med. Sci. Sports 6, 238–241 (1974)Google Scholar
  19. Thomson, J. M., Dempsey, J. A., Chosy, L. W., Shahidi, N. T., Reddan, W. G.: Oxygen transport and oxyhemoglobin dissociation during prolonged muscular work. J. Appl. Physiol. 37 (1974)Google Scholar
  20. Torrance, J. D., Lenfant, C., Cruz, J., Marticorena, E.: Oxygen transport mechanisms in residents at high altitude. Respir. Physiol. 11, 1–15 (1970)Google Scholar
  21. Wranne, B., Nordgren, L., Woodson, R. D.: Increased blood oxygen affinity and physical work capacity in man. Scand. J. Clin. Lab. Invest. 33, 347–352 (1974)Google Scholar

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • J. M. Ramsey
    • 1
  • S. William PipolyJr.
    • 1
  1. 1.Department of BiologyUniversity of DaytonDaytonUSA

Personalised recommendations