Monoclonal IgM radioimmunoassay for hepatitis B surface antigen: high binding activity in serum that is unreactive with conventional antibodies.
Monoclonal IgM radioimmunoassay for hepatitis B surface antigen: high binding activity in serum that is unreactive with conventional antibodies.
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乙型肝炎表面抗原的单克隆 IgM 放射免疫测定：血清中具有高结合活性，与常规抗体不发生反应。
DOI：
10.1073/pnas.79.4.1277
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发表时间：
1982
影响因子：
11.1
通讯作者：
Isselbacher,KJ
中科院分区：
文献类型：
--
作者：
Wands,JR;Bruns,RR;Carlson,RI;Ware,A;Menitove,JE;Isselbacher,KJ
在乙型肝炎放射免疫测定中，我们使用针对乙型肝炎表面抗原 (HBsAg) 的单克隆 IgM 抗体（抗 HBs），在人血清中检测到了高结合活性，而在使用传统抗 HBs 试剂的测定中则没有反应。通过单克隆 IgM 抗 HBs 亲和层析从血清中分离结合材料，并将该材料与 HBsAg 进行比较（通过十二烷基硫酸钠/聚丙烯酰胺凝胶电泳）证明两者共享几种相似的多肽。此外，将 HBsAg 和浓缩单克隆免疫反应材料与常规和单克隆抗 HBs 试剂的结合特性进行比较，证明了一些抗原交叉反应性。单克隆免疫反应材料的分子量约为2 X 10(6)。用单克隆 IgM 抗体对材料进行免疫沉淀，并通过电子显微镜检查，发现结块的“刺状”颗粒，类似于涂有相同抗体的 22 nm 乙型肝炎颗粒。因此，这项研究表明，仅通过单克隆放射免疫测定法在血清中检测到的高结合活性物质与 HBsAg 并不相同，但它具有一些共同的特性。
Using a monoclonal IgM antibody (anti-HBs) to hepatitis B surface antigen (HBsAg) in a radioimmunoassay for hepatitis B, we have detected high binding activity in human serum that was unreactive in assays employing conventional anti-HBs reagents. The binding material was isolated from serum by affinity chromatography on monoclonal IgM anti-HBs, and comparison of the material with HBsAg (by sodium dodecyl sulfate/polyacrylamide gel electrophoresis) demonstrated that the two shared several similar polypeptides. Furthermore, comparison of the binding properties of HBsAg and concentrated monoclonal immunoreactive material with conventional and monoclonal anti-HBs reagents demonstrated some antigenic crossreactivity. The molecular weight of the monoclonal immunoreactive material was approximately 2 X 10(6). Immunoprecipitation of the material with monoclonal IgM antibodies and examination by electron microscopy revealed clumped and "spiculated" particles that resembled 22-nm hepatitis B particles coated with the same antibody. Thus, this study suggests that the high-binding-activity material, detected in serum only by the monoclonal radioimmunoassay, is not identical with HBsAg, but it shares some common properties.