Identification and characterization of allergens in soybeann

IgE结合蛋白（过敏原）的特点是SDS-PAGE和免疫印迹方法使用过敏性皮炎患者的血清。大约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-球蛋白组分中。其中一种分子量约为30，000的特异性蛋白Gly m Bd 30 K与患者血清中的IgE结合最强、最频繁。几乎所有患者血清中均缺乏识别11 S-球蛋白组分中蛋白的IgE，提示该组分中的伴大豆球蛋白可能对特应性皮炎患者的过敏性较低。分离鉴定了大豆34 kDa油体相关蛋白Gly m Bd 30 K。该蛋白与屋尘螨的主要变应原Der p I有30%的同源性。用两种不同的单克隆抗体建立了双抗体夹心ELISA法，可选择性地检测加工食品中Gly m Bd 30 K，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过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.