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• W2045169892 abstract "The nicotinic acetylcholine receptor from Torpedo electric organs is a ligand-gated ion channel that undergoes conformational transitions for activation and/or desensitization. Earlier work suggested that intrinsic fluorescence changes of the receptor monitors kinetic transitions toward the high-affinity, desensitized state. Here, using highly purified membrane preparations to minimize contaminating fluorescence, we examined kinetic mechanisms of the receptor as monitored by its intrinsic fluorescence. Fluorescence changes were specific to the receptor as they were blocked by α-bungarotoxin and were induced by agonists, but not by the antagonist hexamethonium. Acetylcholine, carbamylcholine and suberyldicholine showed only one kinetic phase with relatively fast rates (t1/2 = 0.2–1.2 s). Effective dissociation constants were at least an order of magnitude higher than the high affinity, equilibrium binding constants for these agonists. A semirigid agonist isoarecolone-methiodide, whose activation constant was ∼3-fold lower than acetylcholine, induced an additional slow phase (t1/2 = 4.5–9 s) with apparent rates that increased and then decreased in a concentration dependent manner, revealing a branched mechanism for conformational transitions. We propose that the intrinsic fluorescence changes of the receptor describe a process(es) toward a fast desensitization state prior to the formation of the high affinity state." @default.
• W2045169892 created "2016-06-24" @default.
• W2045169892 creator A5044155455 @default.
• W2045169892 creator A5076765758 @default.
• W2045169892 date "2010-01-31" @default.
• W2045169892 modified "2023-09-25" @default.
• W2045169892 title "Kinetics of agonist-induced intrinsic fluorescence changes in the Torpedo acetylcholine receptor" @default.
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• W2045169892 doi "https://doi.org/10.1093/jb/mvq007" @default.
• W2045169892 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2912032" @default.
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