Kobayashi T, Togashi S, Itoh N, Kumanishi T
Department of Psychiatry, Niigata University School of Medicine, Japan.
J Neuroimmunol. 1995 Mar;57(1-2):129-35. doi: 10.1016/0165-5728(94)00176-o.
In previous work on sigma (sigma) receptors, we established a hybridoma cell line, 10G9, producing a monoclonal anti-idiotypic antibody (anti-Id mAb) to the monoclonal and anti-haloperidol antibody. The anti-Id mAb showed specific binding affinity to sigma receptors in immunoprecipitation and competition experiments. Here we isolated and sequenced cDNA clones for the variable regions of the anti-Id mAb. These combinations of segments and formation of the unique CDR3 were considered to be the structural basis for the diversity of the antigen-binding site of our anti-Id mAb and, therefore, for its binding activity to sigma receptors.
在先前关于σ受体的研究工作中，我们建立了一个杂交瘤细胞系10G9，它能产生针对单克隆抗氟哌啶醇抗体的单克隆抗独特型抗体（抗Id单克隆抗体）。在免疫沉淀和竞争实验中，该抗Id单克隆抗体显示出对σ受体具有特异性结合亲和力。在此，我们分离并测序了抗Id单克隆抗体可变区的cDNA克隆。这些片段的组合以及独特互补决定区3（CDR3）的形成被认为是我们抗Id单克隆抗体抗原结合位点多样性的结构基础，因此也是其与σ受体结合活性的结构基础。
