Cherapakhin V V, Chervonsky A V, Filatov A V, Rokhlin O V
Immunol Lett. 1985;10(3-4):217-21. doi: 10.1016/0165-2478(85)90081-1.
SJL/J mice were immunized with polyclonal rat Ig light chains of two allotypes and immune spleen cells were fused with P3-Ag8.653 myeloma cells. 17 cell populations producing antirat Ig AB were cloned. Four clones, 1G9, L3E8, L2B2 and L2C5 have been characterized in detail. All MABs are of the IgG1, kappa isotype. Using monoclonal rat kappa chains it was demonstrated that all the AB react with rat Ig kappa chains. Further localization of antigenic determinants was performed using isolated L chain C domain. It was shown that all MABs are directed against C domain epitopes. L2C5 MAB binds selectively to August rat L chains, thus showing specificity for Igk-1a determinants. The remaining three clones bind equally well to L chains of different allotypes, but 1G9 clone binds preferentially to isolated L chains as compared to intact IgG molecules.
用两种同种异型的多克隆大鼠Ig轻链免疫SJL/J小鼠，并将免疫脾细胞与P3-Ag8.653骨髓瘤细胞融合。克隆了17个产生抗大鼠Ig AB的细胞群体。详细鉴定了四个克隆，即1G9、L3E8、L2B2和L2C5。所有单克隆抗体均为IgG1、κ同种型。使用单克隆大鼠κ链证明所有AB均与大鼠Igκ链反应。使用分离的L链C结构域对抗原决定簇进行了进一步定位。结果表明所有单克隆抗体均针对C结构域表位。L2C5单克隆抗体选择性结合奥古斯特大鼠L链，从而显示出对Igk-1a决定簇的特异性。其余三个克隆与不同同种异型的L链结合效果相同，但与完整的IgG分子相比，1G9克隆优先结合分离的L链。
