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纯化鳗鱼乙酰胆碱受体及抗乙酰胆碱受体抗体的研究。

Studies on purified eel acetylcholine receptor and anti-acetylcholine receptor antibody.

作者信息

Patrick J, Lindstrom J, Culp B, McMillan J

出版信息

Proc Natl Acad Sci U S A. 1973 Dec;70(12):3334-8. doi: 10.1073/pnas.70.12.3334.

Abstract

Rabbit antiserum against purified Electrophorus electricus acetylcholine receptor is studied using an immunoprecipitin assay to measure either antibody titer or concentration of toxin-binding sites in solubilized receptor preparations. This antiserum, unlike control serum, blocks the electrophysiological response of the electroplax to carbamylcholine. Toxin (alpha-neurotoxin, Naja naja) and several cholinergic ligands produce partial inhibition of the reaction of antiserum with purified acetylcholine receptor. Evidence is presented that some of the toxin-binding sites on receptor, purified by affinity chromatography on toxin-agarose conjugates, are occluded by toxin. In addition, evidence is presented that antireceptor antiserum will cause precipitation of more toxin-binding sites present in an initial extract than in purified receptor preparations.

摘要

利用免疫沉淀试验研究了抗纯化电鳗乙酰胆碱受体的兔抗血清,以测定抗体效价或溶解受体制剂中毒素结合位点的浓度。与对照血清不同,这种抗血清可阻断电鳐对氨甲酰胆碱的电生理反应。毒素(α-神经毒素,眼镜蛇)和几种胆碱能配体可部分抑制抗血清与纯化乙酰胆碱受体的反应。有证据表明,通过毒素-琼脂糖缀合物亲和层析纯化的受体上的一些毒素结合位点被毒素封闭。此外,有证据表明,抗受体抗血清会使初始提取物中存在的毒素结合位点比纯化受体制剂中沉淀出更多。

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Use of affinity chromatography for acetylcholine receptor purification.
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