Rabbit antibodies show unique structural characteristics in that kappa chains have an inter-domain disulfide bond between the variable and constant domains. Here we characterized this disulfide bond from physicochemical viewpoints both in stability and affinity. It was revealed that the disulfide bond contributed to the thermal stability of the antibody, but the affinity and mechanism of antigen recognition was not altered by the mutation. The present result expands the understanding of how rabbit antibodies with kappa light chains gain affinity under characteristic mechanism to gain thermal stability, and would give suggestions for the methods to artificially stabilize antibody molecules.

中文翻译：

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兔免疫球蛋白κ链可变区和恒定区之间的二硫键在热稳定性和亲和力中的作用。

兔抗体显示独特的结构特征，因为κ链在可变域和恒定域之间具有域间二硫键。在这里，我们从稳定性和亲和力两个方面从理化角度表征了该二硫键。揭示了二硫键有助于抗体的热稳定性，但是该突变并未改变抗原识别的亲和力和机理。本结果扩展了对具有κ轻链的兔抗体如何在特征机制下获得亲和力以获得热稳定性的认识，并为人为稳定抗体分子的方法提供了建议。