Barkas T, Gairns J M, Kerr H J, Coggins J R, Simpson J A
Eur J Immunol. 1982 Sep;12(9):757-61. doi: 10.1002/eji.1830120910.
Affinity-purified antibodies to the nicotinic acetylcholine receptor of Torpedo marmorata were fractionated into two populations using a covalently cross-linked receptor-toxin immunosorbent lacking free toxin-binding sites. The population of antibodies which bound to and were subsequently eluted from this resin, and which cannot possibly contain antibodies directed to the toxin-binding site itself, was effective in inhibiting the binding of toxin to receptor in solution. This unequivocally demonstrates that inhibition of toxin binding can be mediated by antibodies which are not directed against the toxin-binding site. A second minor population of antibodies which did not bind to the affinity resin but which did inhibit the binding of toxin to receptor in solution was detected. Two subpopulations of toxin-binding inhibitory antibodies can therefore be distinguished. A clear differentiation should be made in future work describing "anti-toxin site" antibodies between antibodies directly binding to the toxin-binding site and the pseudo-anti-toxin-binding site antibodies described in this report.
利用缺乏游离毒素结合位点的共价交联受体 - 毒素免疫吸附剂，将亲和纯化的斑纹电鳐烟碱型乙酰胆碱受体抗体分为两个群体。与该树脂结合并随后从该树脂上洗脱下来的抗体群体，其不可能含有针对毒素结合位点本身的抗体，该群体在溶液中能有效抑制毒素与受体的结合。这明确表明，毒素结合的抑制可由不针对毒素结合位点的抗体介导。还检测到第二个较小的抗体群体，其不与亲和树脂结合，但在溶液中确实能抑制毒素与受体的结合。因此，可以区分出毒素结合抑制抗体的两个亚群体。在未来描述“抗毒素位点”抗体的工作中，应明确区分直接结合毒素结合位点的抗体与本报告中描述的假抗毒素结合位点抗体。
