Complex Formation between Monoclonal IgM and Albumin.
Complex Formation between Monoclonal IgM and Albumin.
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单克隆 IgM 和白蛋白之间形成复合物。
DOI：
10.1111/j.1365-3083.1974.tb01232.x
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发表时间：
1974
影响因子：
3.7
通讯作者：
I. Følling
中科院分区：
文献类型：
--
作者：
M. Harboe;I. Følling
血清Sö免疫电泳显示异常白蛋白线呈阴极延伸至β区，而较粗的IgM线呈阳极延伸至α2区。这些异常是由白蛋白与单克隆IgM的非共价结合和电泳过程中复合物的持续解离引起的。复合物的形成是免疫特异性的人，而不是牛，白蛋白与IgM结合Sö。IgM‐上的结合位点定位在Fabμ片段上。白蛋白在反应中可能是单价的，因为单个人血清白蛋白结合但不与IgM Sö沉淀，而可溶性人血清白蛋白聚集体与IgM Sö沉淀。
Immunoelectrophoresis of serum Sö showed an abnormal albumin line extended cathodically into the β‐region and a thick IgM line extended anodically into the α2‐region. These abnormalities were caused by noncovalent binding of albumin to a monoclonal IgM and continuous dissociation of the complex during electrophoresis. The complex formation was immunologically specific in that human, hut not bovine, albumin combined with IgM Sö. The combining sites on IgM ‐were localised to the Fabμ fragment. Albumin was probably univalent in the reaction, since monomerk human serum albumin combined but did not precipitate with IgM Sö, whereas soluble aggregates of human serum albumin precipitated with IgM Sö.