Hoffman D R
J Allergy Clin Immunol. 1987 Sep;80(3 Pt 1):300-6. doi: 10.1016/0091-6749(87)90035-2.
Pure venom from Solenopsis invicta was collected by having the insects sting into a capillary tube. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that three major protein bands were present in the venom. A prototype commercial extract was compared and found to contain the three major venom proteins and additional components as well as high potency and specificity by RAST. Immunoblot studies were performed with sera from allergic individuals with blots prepared from denatured SDS-PAGE gels and from two types of nondenaturing gels. The nondenaturing systems demonstrated the presence of two major allergens and three other allergens, each reacting with a third of the sera. Three of the allergens detected in SDS-PAGE blots were of identical mobility to the three major proteins in the pure venom sample. IgE binding to the SDS-PAGE blots was significantly less than that to nondenaturing blots, suggesting that much of the allergenic activity is conformation dependent.
通过让红火蚁叮咬进入毛细管来收集其纯毒液。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)表明毒液中存在三条主要蛋白带。将一种商业化原型提取物进行比较,发现其含有这三种主要毒液蛋白以及其他成分,并且通过放射变应原吸附试验(RAST)显示具有高效能和特异性。使用来自过敏个体的血清进行免疫印迹研究,印迹分别由变性的SDS-PAGE凝胶和两种非变性凝胶制备。非变性系统显示存在两种主要过敏原和其他三种过敏原,每种过敏原与三分之一的血清发生反应。在SDS-PAGE印迹中检测到的三种过敏原与纯毒液样品中的三种主要蛋白具有相同的迁移率。与非变性印迹相比,IgE与SDS-PAGE印迹的结合明显减少,这表明许多过敏活性依赖于构象。