Advertisement

Comparative Immunochemistry of Mammalian Brain and Eel Electric Tissue Acetylcholinesterases

  • A. J. Trevor
  • A. J. Greenberg
Part of the Advances in Behavioral Biology book series (ABBI, volume 24)

Abstract

Acetylcholinesterase (AChE, EC 3.1.1.7) plays an important role in the control of excitability of nerve and muscle tissue via its hydrolytic inactivation of ACh at postsynaptic sites. However, most studies on purified forms of AChE have concerned the enzymes from electric tissues of marine, non-mammalian species (11). AChE has been purified from mammalian brain tissues (2, 16) and while such preparations appear similar in catalytic function to electric tissue enzymes, differences are apparent with respect to molecular size of the enzyme forms (2) and active site numbers (4).

Keywords

Bovine Brain Double Diffusion Brain AChE Bovine Erythrocyte Asymmetric Form 
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.
    Bohlen, P., Stein, S., Dairman, W. and Udenfriend, S. (1973): Arch. Biochem. Biophys. 155:213–220.PubMedCrossRefGoogle Scholar
  2. 2.
    Chan, S. L., Shirachi, D.Y., Bhargava, H. N., Gardner, E. and Trevor, A.J. (1972): J. Neurochem. 19:2747–2758.PubMedCrossRefGoogle Scholar
  3. 3.
    Ellman, G. L., Courtney, K. D., Andres, V. and Featherstone, R. M. (1961): Biochem. Pharmacol. 7:88–95.PubMedCrossRefGoogle Scholar
  4. 4.
    Gordon, M. A., Chan, S. L. and Trevor, A.J. (1976): Biochem. J. 157:69–76.PubMedGoogle Scholar
  5. 5.
    Gurardi, D., Silman, I. and Fuchs, S. (1974): Europ. J. Biochem. 43:179–187.CrossRefGoogle Scholar
  6. 6.
    Holmes, M. J., Michaeli, D. and Fudenberg, H.H. (1973): Immunochemistry 10:461–465.PubMedCrossRefGoogle Scholar
  7. 7.
    Keynes, R. D. (1961): In: Bioelectrogenesis. (Eds.) C. Chagas and A. Paes de Carvaiho, Elsevier Press, New York, pp. 14–19.Google Scholar
  8. 8.
    Levine, L. (1967): In: Handbook of Experimental Immunology, (Ed.) D.M. Weir, Blackwell Sci. Publ., Oxford, pp. 707–719.Google Scholar
  9. 9.
    Ouchterlony, O. (1967): In: Handbook of Experimental Immunology, (Ed.) D. M. Weir, Blackwell Sci. Publ., Oxford, pp. 655–706.Google Scholar
  10. 10.
    Parker, K.K., Chan, S.L. and Trevor, A. J. (1977): Trans. Amer. Soc. Neurochem. 8:170.Google Scholar
  11. 11.
    Rosenberry, T.L. (1975): Adv. Enzymol. 43:103–218.PubMedGoogle Scholar
  12. 12.
    Rossier, J., Baumann, A., Rieger, F. and Benda, P. (1975): In: Cholinergic Mechanisms, (Ed.) P. G. Waser, Raven Press, New York, pp.283–292.Google Scholar
  13. 13.
    Scheidegger, J. J. (1955): Int. Arch. Allergy Appl. Immunol. 7: 103–110.PubMedCrossRefGoogle Scholar
  14. 14.
    Trevor, A.J., Chan, S. L., Gardner, E. and Gordon, M. A. (1976): Proc. West. Pharmacol. Soc. 19:8–12.PubMedGoogle Scholar
  15. 15.
    Williams, R.M. (1969): Proc. Nat. Acad. Sci. USA 62:1175–1180.PubMedCrossRefGoogle Scholar
  16. 16.
    Yamamura, H. I., Reichard, D.W., Gardner, T. L., Morrisett, J. D. and Broomfield, C.A. (1973): Biochim. Biophys. Acta 302: 305–315.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • A. J. Trevor
    • 1
  • A. J. Greenberg
    • 1
  1. 1.Department of Pharmacology, School of MedicineUniversity of CaliforniaSan FranciscoUSA

Personalised recommendations