从结晶毒素复合物中亲和层析纯化A型肉毒杆菌神经毒素。
Affinity chromatography purification of type A botulinum neurotoxin from crystalline toxic complex.
作者信息
Moberg L J, Sugiyama H
出版信息
Appl Environ Microbiol. 1978 May;35(5):878-80. doi: 10.1128/aem.35.5.878-880.1978.
Abstract
Type A botulinum neurotoxin was purified from toxic crystals by adsorption to p-aminophenyl-beta-D-thiogalactopyranoside coupled to CH-Sepharose 4B. At pH 6.3, the toxic complex was held by the binding between the ligand and the hemagglutinin of the complex; the toxin is eluted selectively by dissociating the complex with buffer-saline of pH 7.9. The single-step affinity chromatography recovered 50 to 60% of applied toxicity as preparations of greater than 99% purity.
摘要
通过吸附到偶联于CH-琼脂糖4B的对氨基苯基-β-D-硫代半乳糖吡喃糖苷上，从有毒晶体中纯化出A型肉毒杆菌神经毒素。在pH 6.3时，有毒复合物通过配体与复合物血凝素之间的结合而保持；通过用pH 7.9的缓冲盐水解离复合物来选择性洗脱毒素。单步亲和层析回收了50%至60%的应用毒性，纯度高于99%。
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