Conference paper

The Use of Affinity Gels for the Study of the Ligand Binding Properties of Mammalian Acetylcholinesterase

Gunnar Hollunger ; Department of Pharmacology, University of Umea, S-901 87 Umea, Sweden
Bertil Niklasson ; Department of Pharmacology, University of Umea, S-901 87 Umea, Sweden

Abstract

An affinity adsorption technique for the analysis of the binding
sites of acetylcholinesterase for small ligands is presented. By studying
the interaction of decamethonium and edrophonium the second
anionic binding site of decamethonium ds characterized as
having affinity for trimetyl-(p-aminophenyl)ammonium-CH- Sepharose
4B but not for trimethyl-(m-aminophenyl)ammonium-
CH-Sepharose 4B. The directional localization of a hydrophobic
binding area in the vicinity of the anionic subsite of the catalytic
site is tentatively defined.

Keywords

Hrčak ID:

196618

URI

https://hrcak.srce.hr/196618

Publication date:

3.12.1975.

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