不同的蛋白A免疫吸附剂对大鼠免疫球蛋白可能具有不同的结合特异性。

Different protein A immunosorbents may have different binding specificity for rat immunoglobulins.

作者信息

Nilsson R, Myhre E, Kronvall G, Sjögren H O

出版信息

J Immunol Methods. 1983 Aug 26;62(2):241-5. doi: 10.1016/0022-1759(83)90251-x.

Abstract

Purified polyclonal immunoglobulin preparations representing the 4 rat IgG subclasses were tested for binding to Staphylococcus aureus protein A attached to 3 different solid phases (Staphylococcus aureus Cowan I bacteria, Sepharose CL4B and Sepharose 6MB). Protein A Sepharose CL4B showed higher reactivity with IgG1 and IgG2b than the staphylococci, whereas protein A Sepharose 6MB showed a lower uptake of these subclasses. No differences were seen for IgG2a and IgG2c. Protein A on different solid phases cannot be used interchangeably without confirmation of binding specificity.

摘要

对代表4种大鼠IgG亚类的纯化多克隆免疫球蛋白制剂进行检测，以确定其与附着在3种不同固相（金黄色葡萄球菌考恩I菌、琼脂糖CL4B和琼脂糖6MB）上的金黄色葡萄球菌蛋白A的结合情况。与葡萄球菌相比，蛋白A琼脂糖CL4B对IgG1和IgG2b的反应性更高，而蛋白A琼脂糖6MB对这些亚类的摄取量较低。IgG2a和IgG2c未见差异。在未确认结合特异性的情况下，不同固相上的蛋白A不能互换使用。