小鼠IgG1的异质性：单克隆IgG1抗体与蛋白A-琼脂糖的可变结合。

Mouse IgG1 heterogeneity: variable binding of monoclonal IgG1 antibodies to protein A-sepharose.

作者信息

Villemez C L, Russell M A, Carlo P L

出版信息

Mol Immunol. 1984 Oct;21(10):993-8. doi: 10.1016/0161-5890(84)90158-5.

Abstract

Binding strength to protein A discriminates three definitive types of mouse monoclonal IgG1. Each of these types of IgG1 elutes from protein A-Sepharose as a coherent peak representing the great majority of IgG1 protein. One type of IgG1 is not present to any significant extent in polyclonal mouse IgG preparations, and to our knowledge has not been reported previously. This type of IgG1 does not bind firmly to protein A at pH 8.0, but is retarded sufficiently that it can be purified by protein A-Sepharose chromatography in high yields.

摘要

与蛋白A的结合强度区分出三种确定类型的小鼠单克隆IgG1。每种类型的IgG1从蛋白A-琼脂糖凝胶上洗脱时都呈现为一个连贯的峰，代表了绝大多数的IgG1蛋白。其中一种类型的IgG1在多克隆小鼠IgG制剂中不存在显著含量，据我们所知，此前也未有相关报道。这种类型的IgG1在pH 8.0时不与蛋白A紧密结合，但滞留程度足以通过蛋白A-琼脂糖凝胶层析以高产率进行纯化。