Grubb A O, Zettervall O H
Proc Natl Acad Sci U S A. 1975 Oct;72(10):4115-8. doi: 10.1073/pnas.72.10.4115.
One IgG1(kappa), one IgM(kappa), and one IgA1(kappa) monoclonal (M)-component were purified from one human serum. Rabbit antisera were raised against the IgG and IgM M-components and were absorbed until specific for idiotypic determinants on these molecules. All three M-components gave reactions of immunological identity when tested by double radial immunodiffusion with either of the two idiotype-specific antisera. Both heavy and light chains were isolated from each of the three M-components and all preparations inhibited formation of idiotypic precipitates. None of these preparations formed precipitates with idiotype-specific antisera alone. When heavy or light chains of one M-component were hybridized with light or heavy chains from the other M-components the resultant molecules precipitated with anti-idiotypic serum. Hybrids with chains from polyclonal IgG were not precipitable with such antiserum. These results indicate that the variable region of the heavy chains of these M-components of three different immunoglobulin classes are closely similar, if not identical.
从一份人血清中纯化出一种IgG1(κ链)、一种IgM(κ链)和一种IgA1(κ链)单克隆(M)成分。制备了针对IgG和IgM M成分的兔抗血清,并进行吸收处理,直至对这些分子上的独特型决定簇具有特异性。当用两种独特型特异性抗血清中的任何一种通过双向放射免疫扩散法进行检测时,所有三种M成分均呈现免疫同一性反应。从三种M成分中分别分离出重链和轻链,所有制剂均抑制独特型沉淀物的形成。这些制剂单独与独特型特异性抗血清均不形成沉淀物。当一种M成分的重链或轻链与另一种M成分的轻链或重链杂交时,所得分子可与抗独特型血清形成沉淀。与多克隆IgG的链形成的杂交体不能被这种抗血清沉淀。这些结果表明,这三种不同免疫球蛋白类别的M成分的重链可变区即使不完全相同,也非常相似。