Traunecker A, Dolder B, Karjalainen K
Eur J Immunol. 1986 Jul;16(7):851-4. doi: 10.1002/eji.1830160722.
To obtain antibodies against the individual chains of the T cell receptor (TCR) complex, we have produced chimeric proteins containing domains from immunoglobulin (Ig) and TCR polypeptide chains. Basically, the Ig light chains were used as carriers for the TCR constant (C) region domains. The exons which encode the main body of the C regions of the alpha, beta and the related gamma polypeptide chains were "engineered" into the intronic region between the rearranged Ig variable (V) region and C kappa region genes. All three chimeric genes were expressed in myeloma cells, and the proteins of expected apparent molecular weight were produced. Secreted proteins containing the C beta domain were purified from the culture supernatant by using anti-kappa antibody affinity columns, and two rabbits were then immunized with the purified protein. Both rabbits produced antibodies able to immunoprecipitate the heterodimeric TCR protein.
为了获得针对T细胞受体（TCR）复合物各条链的抗体，我们制备了包含免疫球蛋白（Ig）和TCR多肽链结构域的嵌合蛋白。基本上，Ig轻链被用作TCR恒定（C）区结构域的载体。编码α、β及相关γ多肽链C区主体的外显子被“改造”到重排的Ig可变（V）区和Cκ区基因之间的内含子区域。所有三个嵌合基因均在骨髓瘤细胞中表达，并产生了预期表观分子量的蛋白质。通过使用抗κ抗体亲和柱从培养上清液中纯化出含有Cβ结构域的分泌蛋白，然后用纯化后的蛋白免疫两只兔子。两只兔子均产生了能够免疫沉淀异二聚体TCR蛋白的抗体。
