Dimitrijević L, Radulović M, Cirić B, Odrljin T, Jankov R M, Marzari R
Immunology Research Center, Belgrade, Yugoslavia.
J Immunoassay. 1992;13(2):181-96. doi: 10.1080/15321819208021226.
Y7, a murine monoclonal IgG1 kappa antibody against a human monoclonal IgM lambda DJ molecule, was affinity purified on an IgM lambda immunoaffinity column. As detected by enzyme-linked immunosorbent assay (ELISA) the isolated Y7 monoclonal antibody was shown to be not cross-reactive with human IgG, human secretory IgA, mu chain, lambda + kappa chains and another human monoclonal IgM lambda BR. Binding to the polyclonal human IgM standard in the same assay was about 30 percent. The epitope specificity of affinity purified and biotinylated Y7 MoAb was localized only in the nonreduced pepsin Fab fragments of IgM lambda DJ immunogen. As the immunogen was determined to be a specific antibody to phosphorylcholine, the specificity of Y7 MoAb was further ascertained in its capacity to induce 95% inhibition of immunogen binding for phosphorylcholine.
Y7是一种针对人单克隆IgMλ DJ分子的鼠单克隆IgG1κ抗体,在IgMλ免疫亲和柱上进行了亲和纯化。通过酶联免疫吸附测定(ELISA)检测,分离出的Y7单克隆抗体显示与人IgG、人分泌型IgA、μ链、λ + κ链以及另一种人单克隆IgMλ BR无交叉反应。在同一测定中,与多克隆人IgM标准品的结合率约为30%。亲和纯化并生物素化的Y7单克隆抗体的表位特异性仅定位在IgMλ DJ免疫原的非还原胃蛋白酶Fab片段中。由于确定免疫原为磷酸胆碱的特异性抗体,Y7单克隆抗体的特异性通过其诱导95%抑制免疫原与磷酸胆碱结合的能力进一步得到证实。