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Uncoupling the Sodium Pump

Abstract

IT is now widely accepted that the extrusion of sodium from living cells is associated with the splitting of ATP at the inside surface of the cell membrane1–7. The mechanism responsible is inhibited by cardiac glycosides and it is affected in a complicated way by potassium ions. With membrane preparations from most cells, glycoside-sensitive ATPase activity can be demonstrated only when both sodium and potassium are present5, and in red cells and nerve there is evidence that the sodium ions must be inside and the potassium ions outside6,7. This fits in with the known coupling between sodium efflux and potassium influx in these tissues, and suggests that under normal conditions the transport mechanism catalyses an exchange of sodium ions for potassium ions across the membrane using energy from the hydrolysis of ATP at the internal surface.

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References

  1. Skou, J. C., Biochim. Biophys. Acta, 23, 394 (1957); 42, 6 (1960); 58, 314 (1962).

    Article  CAS  Google Scholar 

  2. Dunham, E. T., and Glynn, I. M., J. Physiol., 156, 274 (1961).

    Article  CAS  Google Scholar 

  3. Post, R. L., Merritt, C. R., Kinsolving, C. R., and Albright, C. D., J. Biol. Chem., 235, 1796 (1960).

    CAS  Google Scholar 

  4. Hoffman, J. F., Fed. Proc., 19, 127 (1960).

    Google Scholar 

  5. Bonting, S. J., Simon, K. A., and Hawkins, N. M., Arch. Biochem., 95, 416 (1961).

    Article  CAS  Google Scholar 

  6. Glynn, I. M., J. Physiol., 160, 18P (1962).

    Google Scholar 

  7. Whittam, R., Biochem. J., 84, 10 (1962).

    Article  Google Scholar 

  8. Glynn, I. M., J. Physiol., 136, 148 (1957).

    Article  CAS  Google Scholar 

  9. Shaw, T. I., Cambridge Univ. Ph.D. dissertation (1954).

  10. Glynn, I. M., J. Physiol., 134, 278 (1956).

    Article  CAS  Google Scholar 

  11. Frumento, A. S., and Mullins, L. J., Nature, 204, 1312 (1964).

    Article  ADS  CAS  Google Scholar 

  12. Keynes, R. D., and Swan, R. C., J. Physiol., 147, 591 (1959).

    Article  CAS  Google Scholar 

  13. Keynes, R. D., J. Physiol., 178, 305 (1965).

    Article  CAS  Google Scholar 

  14. Mullins, L. J., and Frumento, A. S., J. Gen. Physiol., 46, 629 (1963).

    Article  CAS  Google Scholar 

  15. Hoffman, J. F., Tosteson, D. C., and Whittam, R., Nature, 185, 186 (1960).

    Article  ADS  CAS  Google Scholar 

  16. Hoffman, J. F., J. Gen. Physiol., 45, 837 (1962).

    Article  CAS  Google Scholar 

  17. Baker, P. F., Biochim. Biophys. Acta, 88, 458 (1964).

    CAS  PubMed  Google Scholar 

  18. Caldwell, P. C., Hodgkin, A. L., Keynes, R. D., and Shaw, T. I., J. Physiol., 152, 561 (1960).

    Article  CAS  Google Scholar 

  19. Sen, A. K., and Post, R. L., J. Biol. Chem., 239, 345 (1964).

    CAS  PubMed  Google Scholar 

  20. Whittam, R., and Ager, M. E., Biochem. J. (in the press).

Download references

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GARRAHAN, P., GLYNN, I. Uncoupling the Sodium Pump. Nature 207, 1098–1099 (1965). https://doi.org/10.1038/2071098a0

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