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Change in the intrinsic fluorescence of acetylcholine receptor purified from Narke japonica upon binding with cholinergic ligands
Authors:Norio Kaneda  Fumio Tanaka  Michiaki Kohno  Kyozo Hayashi  Kunio Yagi
Affiliation:1. Institute of Biochemistry, Faculty of Medicine, University of Nagoya, Nagoya 466, U.S.A.;1. Department of Biophysics, Institute for Virus Research, Kyoto University, Kyoto 606, Japan;3. Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Kyoto 606, Japan
Abstract:Effects of various cholinergic ligands on the intrinsic fluorescence of acetylcholine receptor purified from the electric organ of Narke japonica were investigated. Binding with acetylcholine decreased the fluorescence by 7–8%, and that with carbamylcholine by 4–5% at 20 °C. Decamethonium and d-tubocurarine did not affect significantly the fluorescence intensity, while hexamethonium enhanced it. These changes were completely inhibited by preincubation of the receptor with α-bungarotoxin, which indicated that the observed intrinsic fluorescence change was due to the specific binding of each ligand. Data of the quenching experiment using iodide ion as an extrinsic quencher suggested the occurrence of the conformational change in the receptor upon binding with various cholinergic ligands. Considering these results together with those on intrinsic fluorescence change, conformational change provoked by binding with acetylcholine or carbamylcholine seems to differ from that provoked by binding with other cholinergic ligands examined.
Keywords:To whom correspondence should be addressed.
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