Advertisement

Acetylcholinesterase and Butyrylcholinesterase: Similarities in Normal and Denervated Muscles, Differences in Axonal Transport

  • L. di Giamberardino
  • J. Y. Couraud
Part of the Advances in Behavioral Biology book series (ABBI, volume 25)

Abstract

Acetylcholinesterase (AChE: EC 3.1.1.7) and butyrylcholinesterase (BuChE: EC 3.1.1.8) are two enzymes distinguishable by substrate specificity (12,14), inhibitors sensitivity (14) and, more recently, by immunological properties (16) and thermal stability (8,16). In spite of many distinct properties, the two enzymes are often found together (3) and show analogous structure (11,16) and similar behavior in some instances (13).

Keywords

Sciatic Nerve AChE Activity Axonal Transport Molecular Form Sucrose Gradient 
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. 1.
    Couraud, J.Y. and Di Giamberardino, L. (1980): J. Neurochem. 35:1063–1066.CrossRefGoogle Scholar
  2. 2.
    Couraud, J.Y., Koenig, M. and Di Giamberardino, L. (1980): J. Neurochem. 34:1209–1218.CrossRefGoogle Scholar
  3. 3.
    Davis, R. and Koelle, G. (1978): J. Cell Biol. 78:785–809.CrossRefGoogle Scholar
  4. 4.
    Di Giamberardino, L. and Couraud, J.Y. (1978): Nature 271:170–172.CrossRefGoogle Scholar
  5. 5.
    Di Giamberardino, L., Couraud, J.Y. and Barnard, E.A. (1979): Brain Res. 160:196–202.CrossRefGoogle Scholar
  6. 6.
    Fernandez, H.L., Duell, M.J. and Festoff, B.W. (1980): J. Neurochem. 11:31–39.Google Scholar
  7. 7.
    Hall, Z. (1973): J. Neurobiol. 4:346–361.CrossRefGoogle Scholar
  8. 8.
    Koelle, G.B., Kitto Rickard, K. and Ruch, G.A. (1979): Proc. Nat. Acad. Sci. 76:6012–6016.CrossRefGoogle Scholar
  9. 9.
    Lomo, T. (1980): Trends Neurosci. 23:126–129.CrossRefGoogle Scholar
  10. 10.
    Lyles, J.M. and Barnard, E.A. (1980): FEBS Lett. 109:9–12.CrossRefGoogle Scholar
  11. 11.
    Lyles, J.M., Silman, I. and Barnard, E.A. (1979): J. Neurochem. 33:727–738.CrossRefGoogle Scholar
  12. 12.
    Meyers, D.K. (1953): Biochem. J. 55: 67–79.Google Scholar
  13. 13.
    Silman5 I., Di Giamberardino, L., Lyles, J., Couraud, J.Y. and Barnard, E.A. (1979): Nature 280:160–162.CrossRefGoogle Scholar
  14. 14.
    Silver, A. (1974): The Biology of Cholinesterases, North- Holland, Amsterdam.Google Scholar
  15. 15.
    Vigny, M., Di Giamberardino, L., Couraud, J.Y., Rieger, F. and Koenig, J. (1976): FEBS Lett. 69:277–280.CrossRefGoogle Scholar
  16. 16.
    Vigny, M., Gisiger, V. and Massoulie, J. (1978): Proc. Nat. Acad. Sci. 75:2588–2592.CrossRefGoogle Scholar
  17. 17.
    Vigny, M., Koenig, J. and Rieger, F. (1976): J. Neurochem. 27:1347–1353CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1981

Authors and Affiliations

  • L. di Giamberardino
    • 1
  • J. Y. Couraud
    • 1
  1. 1.Department of BiologyC.E.A. de SaclayGif-Sur-YvetteFrance

Personalised recommendations