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Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membranes

机译:从电泳电膜中纯化与河豚毒素结合的河豚毒素结合成分

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摘要

The tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from electroplax membranes of Electrophorus electricus has been purified. The toxin-binding site could be efficiently solubilized with Lubrol-PX, resulting in an extract of high initial specific activity. Purification was facilitated by the development of a rapid, quantitative binding assay. The binding component was stabilized during purification by the use of mixed lipid/detergent micelles of defined composition, and by the saturation of the site with tetrodotoxin. The purification was achieved by means of a highly selective adsorption of the toxin-binding component to DEASE-Sephadex A-25, followed by desorption at high ionic strength and chromatography over Sepharose 6B. Final peak specific activities were at least 50% of the specific activity expected for a pure, undenatured toxin-binding componenet of 230,000 molecular weight. The purified material exhibited a sedimentation coefficient of approximately 8 S and an unusual Stokes radius of 95 A. Purified material showed a relatively simple pattern on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, being comprised of only three polypeptides.
机译:已纯化了与来自电泳的电泳膜的电压敏感钠通道相关的河豚毒素结合成分。毒素结合位点可以被Lubrol-PX有效地溶解,从而得到高初始比活度的提取物。快速定量结合试验的发展促进了纯化。通过使用确定的组成的混合脂质/洗涤剂胶束,以及通过河豚毒素使位点饱和,可以在纯化过程中稳定结合成分。通过将毒素结合组分高度选择性地吸附到DEASE-Sephadex A-25上,然后在高离子强度下进行解吸并在Sepharose 6B上进行色谱分离来实现纯化。最终峰的比活度至少是230,000分子量的纯的,未变性的毒素结合组分所预期的比活度的50%。纯化的材料显示出约8 S的沉降系数,异常斯托克斯半径为95A。纯化的材料在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳上显示出相对简单的图案,仅包含三个多肽。

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