Identification and characterization of allergens in soybeann

采用SDS-PAGE和免疫印迹方法对特应性皮炎患者血清中的ige结合蛋白（过敏原）进行了表征。约15种大豆蛋白组分被患者的sers识别，其中约三分之二被分配到7s -球蛋白部分的组分。一种分子量约为30,000的独特蛋白质与患者的IgEs结合最强烈，最频繁，被命名为Gly m Bd 30K。几乎所有患者的血清都缺乏识别11s -球蛋白部分蛋白的ige，提示该部分蛋白conglycin可能对特应性皮炎患者的致敏性较低。主要过敏原Gly m b30k被分离鉴定为大豆油体相关蛋白（340kda）。该蛋白与屋尘螨的主要过敏原Der p I序列同源性约为30%。采用两种不同的单克隆体，建立了夹心酶联免疫吸附法（ELISA），可选择性测定加工食品中的Gly m b30k，灵敏度在5 ~ 500 ng之间。本研究结果可为食品过敏患者开发低致敏性大豆食品提供参考。

IgE-Binding proteins (allergens) have been characterized by SDS-PAGE and immunoblot methods using sera of the patients with atopic dermatisis. About 15 components of soybean proteins were recognized by patient's sers and about two-thirds of them were assigned to the components in the 7S-globulin fraction. A unique protein with a molecular weight of about 30,000 bound most strongly and frequently with the patient's IgEs, which was named as Gly m Bd 30K.Sera of almost all the patients were shown to lack the IgEs recognizing the proteins in 11S-globulin fraction, suggesting that the proteins in this fraction, conglycinin, may be less allergenic to the patients with atopic dermatisis. The major allergen, Gly m Bd 30K, was isolated and identified to be soybean 34-kDa oil-body-associated protein. This protein was shown to have about 30% sequence homology with Der p I, the major allergen of house dust mite. Using two distinct moncobdies, the sandwich ELISA was developed for the selective determination of Gly m Bd 30K in the processed foods with the sensitivity between 5 and 500 ng. The results obtained in the present investigation may provide useful knowledges for the development of hypoallergenic soybean foods to the food-allergic patients.