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应用两种不同的表达系统对FceR I α亚基的细胞外区进行克隆和表达,表达产物经纯化后用免疫斑点杂交法检测其与IgE结合的能力,探索IgE与其高亲和力受体FceR I α亚基的细胞外区结合的机制。结果两种体系均成功表达出FceRI α亚基的细胞外区,pBAD/gⅢA表达的FceR I α亚基的细胞外区能与IgE结合,而PQE30表达的FeaR I α亚基的细胞外区不能与IgE结合。提示FccR I α亚基的细胞外区已足够和IgE结合,无需β、γ亚基的存在,其所具有的一定的空间构型和二硫键的形成在与IgE结合时是必需的,而糖基化位点在与IgE的结合时是非必需的。
Two different expression systems were used to clone and express the extracellular domain of FceR I α subunit. The expressed product was purified and its ability of binding to IgE was detected by immunoblotting. The relationship between IgE and its high affinity receptor FceR I α Mechanism of subunit extracellular domain binding. Results The extracellular domain of FceRI α subunit was successfully expressed in both of the two systems. The extracellular domain of FceR I α subunit expressed by pBAD / g Ⅲ A could bind to IgE, while the extracellular domain of FeaR I α subunit expressed by PQE30 could not Binds to IgE. It is suggested that the extracellular domain of FccR I α subunit is enough to bind to IgE without the presence of β and γ subunits. It has certain spatial configuration and disulfide bond formation necessary for IgE binding. Glycosylation sites are not necessary for binding to IgE.