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通常的免疫球蛋白制品含>99%IgG,仅有微量的IgA、IgM和含25-40%的IgG二聚体。而特异性免疫球蛋白中也含有少量的二聚体(5-20%)。大约40年前Oncley等人首先报告了免疫球蛋白存在IgG二聚体,他们根据超离心测定结果,提出二聚体是由二个IgG分子末端与末端相连而成。自此以后,发表了许多关于二聚体研究的报导。但是无人弄清二聚体形成的机理。某些研究者认为二聚体是由于使用乙醇在分离过程中,IgG分子部分变性所引起的,用离子交换层析法制备的
Typical immunoglobulin preparations contain> 99% IgG with only traces of IgA, IgM and 25-40% IgG dimers. While specific immunoglobulins also contain small amounts of dimers (5-20%). About 40 years ago, Oncley et al. First reported the presence of IgG dimers in immunoglobulins. According to the results of the ultracentrifugation assay, they suggested that the dimer was formed by linking the ends of two IgG molecules to each other. Since then, many reports on dimer research have been published. However, no one knows the mechanism of dimer formation. Some researchers believe that dimers are due to the partial denaturation of IgG molecules during the isolation process using ethanol, prepared by ion exchange chromatography