Friguet B, Djavadi-Ohaniance L, Goldberg M E
Mol Immunol. 1984 Jul;21(7):673-7. doi: 10.1016/0161-5890(84)90053-1.
Recent studies with monoclonal antibodies directed against different epitopes of the beta 2-subunit of Escherichia coli tryptophan synthase have shown that some of these antibodies bind rapidly in solution to the native protein; others bind very slowly to native beta 2 in solution while they recognize quite rapidly this antigen adsorbed on a microtitration plate. In the present work, an enzyme-linked immunosorbent assay competition test with either the native or a denatured form of the antigen has been developed. It allowed us to show that the rapidly binding antibodies recognize epitopes present on the native protein while those which react very slowly in solution bind preferentially to the denatured form of the protein. These results prompted us to emphasize how important it is, in the characterization of antibodies, to ascertain that the antigen they recognize remains native in the specificity test.
最近针对大肠杆菌色氨酸合酶β2亚基不同表位的单克隆抗体研究表明，其中一些抗体在溶液中能迅速与天然蛋白结合；另一些抗体在溶液中与天然β2结合非常缓慢，而它们能相当迅速地识别吸附在微量滴定板上的这种抗原。在本研究中，我们开发了一种使用天然或变性抗原形式的酶联免疫吸附测定竞争试验。这使我们能够表明，快速结合的抗体识别天然蛋白上存在的表位，而那些在溶液中反应非常缓慢的抗体则优先结合蛋白的变性形式。这些结果促使我们强调，在抗体表征中，确定它们识别的抗原在特异性测试中保持天然状态是多么重要。
