Glaser M, Singer S J
Proc Natl Acad Sci U S A. 1971 Oct;68(10):2477-9. doi: 10.1073/pnas.68.10.2477.
The reversible binding of the haptens 2,4-dinitrophenyllysine (DNP-lysine) and 2,4,6-trinitrophenyllysine (TNP-lysine) to either the nitrophenyl-binding myeloma protein MOPC-315 or to pooled mouse anti-DNP or anti-TNP antibodies produces large and characteristic extrinsic Cotton effects (in the circular dichroic spectra). Despite the similarities in binding characteristics of the three proteins, the circular dichroic spectra produced by the haptens bound to the active sites of these proteins were markedly different. Extrinsic Cotton effects, therefore, provide a powerful new probe of the structure of the reversible complex formed between a hapten and an antibody active site.
半抗原2,4-二硝基苯赖氨酸(DNP-赖氨酸)和2,4,6-三硝基苯赖氨酸(TNP-赖氨酸)与硝基苯结合性骨髓瘤蛋白MOPC-315或与混合的小鼠抗DNP或抗TNP抗体的可逆结合,会产生大的且具有特征性的外在科顿效应(在圆二色光谱中)。尽管这三种蛋白质在结合特性上有相似之处,但半抗原与这些蛋白质活性位点结合所产生的圆二色光谱却明显不同。因此,外在科顿效应为研究半抗原与抗体活性位点之间形成的可逆复合物的结构提供了一种强大的新探针。