Studies of nicotinic acetylcholine receptor protein from rat brain: II. Partial purification
作者： William M. Moore , Robert N. Brady
DOI: 10.1016/0304-4165(77)90271-9
关键词: Nicotine 、 Chloride 、 Affinity chromatography 、 Biochemistry 、 Alpha-4 beta-2 nicotinic receptor 、 Ligand (biochemistry) 、 Chromatography 、 Nicotinic acetylcholine receptor 、 Receptor 、 Acetylcholine receptor 、 Chemistry
摘要: Abstract The pharmacological specificity of the binding 125 I-labeled α-bungarotoxin to a 1% Emulphogene BC-720 extract rat brain particulate fraction has been investigated. contains component which possesses characteristics nicotinic acetylcholine receptor protein. crude soluble protein was purified by affinity chromatography utilizing α-neurotoxin Naja naja siamensis as ligand and 1.0 M carbamylcholine chloride eluant. A single, batch-wise, procedure yields an average purification 510-fold. When this material is treated second time chromatography, high 12 600-fold obtained. Binding saturable with K d 1·10 −8 M. Nicotine iodide at concentrations 10 −5 inhibit toxin-acetylcholine complex formation 41 61% respectively. At −4 M, (+)-tubocurarine give respectively 52 82% inhibition. Eserine sulfate atropine have no effect on concentration These data support isolation partially
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