Kunkel H G, Posnett D N, Pernis B
Ann N Y Acad Sci. 1983;418:324-9. doi: 10.1111/j.1749-6632.1983.tb18082.x.
The anti-gamma globulins represent a very heterogeneous group of proteins with widely different specificities that might be considered a portion of the immune network. The hypothesis is presented that at least some of these proteins have other specificities, with the anti-gamma globulin reactivity being a secondary property. Anti-idiotypic antibodies are possible candidates. This is based on the low binding affinity for gamma globulin of many of these proteins and the results of CRI and sequence studies. All the proteins of the major CRI group have VKIIIb light chains, and these have a dominant but not total influence on this CRI. This has been evident from studies with rabbit antibodies and recently also with monoclonal hybridoma antibodies. Sequence studies have also demonstrated the similarity in light chains that, however, are not greater than with other VKIIIb chains; the heavy chains show little similarity except possibly in the J segment. The possibility is discussed that antibodies with secondary anti-gamma globulin binding properties might have selective advantages.
抗γ球蛋白代表了一组非常异质的蛋白质,其特异性差异很大,可能被视为免疫网络的一部分。有人提出这样的假说,即这些蛋白质中至少有一些具有其他特异性,而抗γ球蛋白反应性是其次要特性。抗独特型抗体可能是候选者。这是基于许多此类蛋白质对γ球蛋白的低结合亲和力以及CRI和序列研究的结果。主要CRI组的所有蛋白质都有VKIIIb轻链,这些轻链对这种CRI有主要但并非完全的影响。这从用兔抗体以及最近用单克隆杂交瘤抗体进行的研究中可以明显看出。序列研究也证明了轻链的相似性,但这种相似性并不比与其他VKIIIb链的相似性更大;重链除了在J段可能有一点相似性外,几乎没有相似之处。文中讨论了具有次要抗γ球蛋白结合特性的抗体可能具有选择性优势的可能性。