Changes of the conformation of rabbit IgG antibody caused by the specific binding of a hapten. X-ray small-angle studies.
Changes of the conformation of rabbit IgG antibody caused by the specific binding of a hapten. X-ray small-angle studies.
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半抗原特异性结合引起兔 IgG 抗体构象的变化。
DOI：
10.1111/j.1432-1033.1974.tb03247.x
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
F. Karush
中科院分区：
文献类型：
--
作者：
I. Pilz;O. Kratky;F. Karush
用小角X射线散射法研究了对偶氮苯基-β-乳糖苷特异性兔抗体的构象，并评价了与半抗原的相互作用效果。半抗原与抗体的结合引起蛋白质构象的变化。实验结果表明，当结合位点的50%被占据时，由于与半抗原的相互作用，抗体的回转半径和体积减小2 - 3%。由于散射曲线的典型形状保持不变，因此推断构象的变化主要由体积收缩组成，而最好由T形模型描述的整体形状基本上没有改变。
The conformation of rabbit antibody specific for the ρ-azophenyl-β-lactoside group was studied by small-angle X-ray scattering and the effect of interaction with hapten evaluated. The binding of hapten to the antibody caused a change in the conformation of the protein. The experimental findings indicate that the radius of gyration and the volume of the antibody become smaller by 2 to 3% as a result of interaction with hapten when 50% of the combining sites are occupied. Since the typical shape of the scattering curves remains the same it is inferred that the change of conformation consists mainly of a volume contraction whereas the overall shape, which is best described by T-shaped models, is not essentially modified.