Rockey J H, Freed R M
Scand J Immunol. 1976;5(6-7):655-66. doi: 10.1111/j.1365-3083.1976.tb03015.x.
Extrinsic Cotton effects generated by binding haptens to native and reformed MOPC-315 protein, its subunits, and its Fv fragment have been examined. The identity of the combining sites of native and reassociated proteins and Fv-315 was demonstrated by the identity of their circular dichroism (CD) difference spectra. The spectrum of TNP-aminocaproate complexed with L chains differed in maxima and minima and cross-over points and lacked the 495-nm CD peak of TNP-aminocaproate-MOPC-315 protein and Nalpha-TNP-tryptophan spectra. A negative 293-nm tryptophanyl CD band, present in spectra of MOPC-315 protins and Fv-315 but absent from spectra of L and H chains, was blue-shifted by haptens and may represent electronic interactions occurring within the MOPC-315 combining site between tryptophanyl and chromophoric residues of different subunits. This conclusion is supported by molecular models of the MOPC-315 combining site.
已经研究了通过将半抗原与天然和重组的MOPC - 315蛋白、其亚基及其Fv片段结合而产生的外在棉花效应。天然和重新缔合的蛋白质以及Fv - 315的结合位点的一致性通过它们的圆二色性（CD）差光谱的一致性得以证明。与轻链复合的TNP - 氨基己酸的光谱在最大值、最小值和交叉点上有所不同，并且缺乏TNP - 氨基己酸 - MOPC - 315蛋白和Nα - TNP - 色氨酸光谱的495 nm CD峰。在MOPC - 315蛋白和Fv - 315的光谱中存在的负293 nm色氨酸CD带，而在轻链和重链的光谱中不存在，被半抗原蓝移，并且可能代表在MOPC - 315结合位点内不同亚基的色氨酸残基和发色团残基之间发生的电子相互作用。这一结论得到了MOPC - 315结合位点的分子模型的支持。
