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Part of the book series: Advances in Behavioral Biology ((ABBI,volume 24))

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Abstract

Constitutents of acetylcholinesterase (AChE; EC 3.1.1.7) amino acids and carbohydrates were determined from highly purified enzyme. AChE was prepared from the electric organ of Torpedo marmorata. For transportation and storage the dissected organs were deep frozen at -30°. Even after a year we could not detect any loss of enzyme activity. As AChE is bound to synaptic membranes, only a small amount of enzyme was obtained after homogenization with conventional buffer solutions. Rothenberg and Nachmansohn (7) suggested the use of toluene to obtain higher enzyme yield. The lipids of the tissue are dissolved with toluene and one can assume that the enzyme is linked to the synaptic membrane by lipids. Although the lipids are not direct constituents of AChE we classified them under constituents because of their close association with the enzyme. For this reason, in collaboration with Dr. Heinrich Muldner (Max-Planck Institute for Biophysical Chemistry, Gottingen, Germany), we prepared and analyzed the lipids.

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© 1978 Plenum Press, New York

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Werner, G., Wojnarowski, W., Hopff, W.H., Waser, P.G. (1978). Constituents of Acetylcholinesterase. In: Jenden, D.J. (eds) Cholinergic Mechanisms and Psychopharmacology. Advances in Behavioral Biology, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3096-7_16

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  • DOI: https://doi.org/10.1007/978-1-4684-3096-7_16

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3098-1

  • Online ISBN: 978-1-4684-3096-7

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