Hoffman D R, Dove D E, Jacobson R S
Department of Pathology, East Carolina University School of Medicine, NC 27858-4354.
J Allergy Clin Immunol. 1988 Nov;82(5 Pt 1):818-27. doi: 10.1016/0091-6749(88)90084-x.
Commercial Solenopsis invicta (Sol i) venom was fractionated by gel filtration and high-performance cation exchange chromatography. Four proteins were isolated and purified to homogeneity. The four proteins were tested with a panel of sera from patients allergic to fire ant venom; all proteins had significant allergenic activity. These proteins corresponded to four of the bands we previously reported to be allergenic by immunoblot analysis. Sol i I has an apparent molecular weight of 37,000 daltons and yields bands of 18,000, 16,500 and 14,000 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis; cation-exchange chromatography indicates that there are three charge forms. Sol i II has a native molecular weight of 28,000 daltons and appears to be easily cleaved into half molecules; it is a phospholipase structurally unlike either bee or wasp phopholipases. Sol i III has a native and denatured molecular weight of 26,000 daltons. Sol i IV has an apparent native molecular weight of 20,000 daltons and gives a single chain of 15,000 daltons in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sol i II and III are the major proteins in the venom; there are only small amounts of Sol i I and IV. All are significant allergens, and patients are found who react most strongly with each. Regression analysis of RAST data with highly purified allergens indicated that the IgE responses to the allergens were not related to each other. Amino acid compositions indicated that the four allergens were distinct and that the allergens were structurally different from each other. Four proteins identical to Sol i I to IV were isolated from hand-milked pure venom.
商业红火蚁（Sol i）毒液通过凝胶过滤和高效阳离子交换色谱进行分离。分离并纯化出四种蛋白质，使其达到均一性。用一组对火蚁毒液过敏患者的血清对这四种蛋白质进行检测；所有蛋白质都具有显著的致敏活性。这些蛋白质与我们之前通过免疫印迹分析报告具有致敏性的四条条带相对应。Sol i I的表观分子量为37,000道尔顿，在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中产生18,000、16,500和14,000道尔顿的条带；阳离子交换色谱表明存在三种电荷形式。Sol i II的天然分子量为28,000道尔顿，似乎很容易裂解为半分子；它是一种磷脂酶，在结构上与蜜蜂或黄蜂的磷脂酶不同。Sol i III的天然和变性分子量均为26,000道尔顿。Sol i IV的表观天然分子量为20,000道尔顿，在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中产生一条15,000道尔顿的单链。Sol i II和III是毒液中的主要蛋白质；Sol i I和IV的含量很少。所有这些都是重要的过敏原，并且发现有患者对每种过敏原反应最为强烈。用高度纯化的过敏原对放射性过敏原吸附试验（RAST）数据进行回归分析表明，对这些过敏原的IgE反应彼此不相关。氨基酸组成表明这四种过敏原各不相同，且它们在结构上彼此不同。从手工采集的纯毒液中分离出了与Sol i I至IV相同的四种蛋白质。
