Advertisement

The haemoglobin molecule as a model drug receptor

  • P. J. Goodford
Part of the Biological Council book series (BCSDA)

Abstract

It is nearly a century since Langley (1878) suggested that there might be a substance in nerves or glands with which atropine and pylocarpine could combine. He was studying salivary secretion, and was attempting to interpret his observations according to the concepts of Guldberg and Waage (1864), who had recently proposed the Law of Mass Action. This Law was very attractive to Langley because it allowed him to formulate his ideas quantitatively, and many investigations of drug action have been interpreted along similar lines during the past 100 years. Such work may all be regarded as the logical extension of Langley’s pioneering studies, and it is appropriate that he should be remembered at this Symposium on Drug Action at the Molecular Level.

Keywords

Electron Spin Resonance Receptor Site Dissociation Curve Oxygen Affinity Beta Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adair, G. S., Barcroft, J. and Bock, A. V. (1921). J. Physiol., 55, 332PubMedPubMedCentralCrossRefGoogle Scholar
  2. Allen, D. W., Guthe, K. F. and Wyman, J. Jr. (1950). J. Biol. Chem., 187, 393PubMedGoogle Scholar
  3. Arnone, A. (1972). Nature (London), 237, 146CrossRefGoogle Scholar
  4. Barcroft, J. and Haldane, J. S. (1902). J. Physiol., 28, 232PubMedPubMedCentralCrossRefGoogle Scholar
  5. Barcroft, J. and Roberts, Ff. (1909). J. Physiol., 39, 143PubMedPubMedCentralCrossRefGoogle Scholar
  6. Beddell, C. R., Goodford, P. J., Norrington, F. E., Wilkinson, S. and Wootton, R. (1976). Br. J. Pharmacol., 57, 201PubMedPubMedCentralCrossRefGoogle Scholar
  7. Benesch, R., Benesch, R. E. and Yu, C. I. (1968). Proc. Nat. Acad. Sci. U.S.A., 59, 526CrossRefGoogle Scholar
  8. Bohr, C. (1909). Nagels Handbuch, Vol. 1, p. 73Google Scholar
  9. Bragg, W. L. (1913). Proc. R. Soc. London A, 89, 248CrossRefGoogle Scholar
  10. Chanutin, A. and Curnish, R. R. (1967). Arch. Biochem. Biophys., 121, 96PubMedCrossRefGoogle Scholar
  11. Douglas, C. G., Haldane, J. S. and Haldane, J. B. S. (1912). J. Physiol., 44, 275PubMedPubMedCentralCrossRefGoogle Scholar
  12. Drabkin, D. L. (1946). J. Biol. Chem., 164, 703PubMedGoogle Scholar
  13. Good, N. E., Winget, G. D., Winter, W., Connolly, T. N., Izawa, S. and Singh, R. M. M. (1966). Biochemistry, 5, 467PubMedCrossRefGoogle Scholar
  14. Goodford, P. J. (1973). Adv. Pharmacol. Chemother., 11, 51PubMedCrossRefGoogle Scholar
  15. Greenwald, I. (1925). J. Biot Chem., 63, 339Google Scholar
  16. Guldberg, C. M. and Waage, P. (1864). Les Mondes, 5, 107Google Scholar
  17. Jeffrey, G. A. (1946). Proc. R. Soc. London A, 1946–47, 188, 222Google Scholar
  18. Kendrew, J. C., Watson, H. C., Strandberg, B. E., Dickerson, R. E., Phillips, D. C. and Shore, V. C. (1961). Nature (London), 190, 666Google Scholar
  19. Langley, J. N. (1878). J. Physiol., 1, 339PubMedPubMedCentralCrossRefGoogle Scholar
  20. Langley, J. N. (1905). J. Physiol., 33, 374PubMedPubMedCentralCrossRefGoogle Scholar
  21. Matsuda, G., Gehring-MtIller, R. and Braunitzer, G. (1963). Biochem. Z., 338, 669PubMedGoogle Scholar
  22. Norrington, F. E. (1974). Lab. Pract., April 191Google Scholar
  23. Ostwald, W. (1908). Z. Chem. Ind. Koll., 11, 264CrossRefGoogle Scholar
  24. Paterson, R. A., Eagles, P. A. M., Young, D. A. B. and Beddell, C. R. (1976). Int. J. Biochem., 7, 117CrossRefGoogle Scholar
  25. Perutz, M. F., Muirhead, H., Cox, J. M. Goaman, L. C. G., Mathews, F. S., McGandy, E. L. and Webb, L. E. (1968). Nature (London), 219, 29CrossRefGoogle Scholar
  26. Rapoport, S. and Guest, G. M. (1941). J. Biol. Chem., 138, 269Google Scholar
  27. Robertson, J. M. (1934). Proc. R. Soc. London A, 146, 473CrossRefGoogle Scholar
  28. Roughton, F. J. W. (1949). Obituary Notices of Fellows of the Royal Society, 6, 315CrossRefGoogle Scholar
  29. Sheppard, W. A. and Boums, A. N. (1954). Can. J. Chem., 32, 4CrossRefGoogle Scholar
  30. van Slyke, D. D. and Neill, J. M. (1924). J. Biol. Chem., 61, 523Google Scholar
  31. Stamatoyannopoulos, G. (1972). Ann. Rev. Genet., 6, 47PubMedCrossRefGoogle Scholar
  32. Sugita, Y. and Chanutin, A. (1963). Proc. Soc. Exp. Biol. Med., 112, 72PubMedCrossRefGoogle Scholar
  33. Williams, R. C. Jr. and Tsay, K-Y. (1973). Anal. Biochem., 54, 137PubMedCrossRefGoogle Scholar

Copyright information

© Institute of Biology Endowment Trust Fund 1977

Authors and Affiliations

  • P. J. Goodford
    • 1
  1. 1.The Wellcome Research LaboratoriesBeckenham, KentUK

Personalised recommendations