Inganäs M, Johansson S G, Bennich H H
Scand J Immunol. 1980;12(1):23-31. doi: 10.1111/j.1365-3083.1980.tb00037.x.
The peptic fragments F(ab')2 and Fc" of human polyclonal IgE were tested by the SpA-IgE radioimmunoassay for interaction with protein A from Staphylococcus aureus. The Fab'2 epsilon fragment but not the Fc" epsilon fragment retained the ability to react with protein A. IgG preparations from different species were tested for ther capacity to inhibit the reaction between 125I-IgE and protein A. IgG preparations from man and the dog, pig, guinea-pig and rhesus monkey were all potent inhibitors whereas those from the rabbit, rat, sheep, horse, cow, goat and mouse were very poor inhibitors. The inhibition of the binding of 125I-IgE to protein A by Fab'2 gamma fragments, but not by Fc gamma fragments, suggests a novel type of interaction of protein A with immunoglobulins.
通过葡萄球菌A蛋白 - IgE放射免疫测定法检测人多克隆IgE的消化片段F(ab')2和Fc"与金黄色葡萄球菌蛋白A的相互作用。Fab'2ε片段而非Fc"ε片段保留了与蛋白A反应的能力。检测了来自不同物种的IgG制剂抑制125I - IgE与蛋白A之间反应的能力。来自人和狗、猪、豚鼠及恒河猴的IgG制剂都是强效抑制剂,而来自兔、大鼠、绵羊、马、牛、山羊和小鼠的IgG制剂则是非常弱的抑制剂。Fab'2γ片段而非Fcγ片段对125I - IgE与蛋白A结合的抑制作用表明蛋白A与免疫球蛋白之间存在一种新型相互作用。