Skoczowski Andrzej, Obtułowicz Krystyna, Czarnobilska Ewa, Dyga Wojciech, Stachowicz Maria, Waga Jacek
Przegl Lek. 2013;70(12):1043-7.
Gliadins and glutenins--the main components of wheat gluten--are highly complex and polymorphic proteins of wheat kernels. They are also allergenic proteins causing a range of food allergies. We hypothesized that the diversity of chemical structures and properties may relate to the diversification of immunoreactive properties of various subunits and fractions of gluten proteins. In the present study we used IgE sera, obtained from patients manifesting different symptoms of wheat allergies, for immunobloting analysis, to prove the specificity of immunological reaction between IgE antibodies and individual gliadins and glutenins, separated by SDS-PAGE. The results suggest that patients have different characteristics of IgE binding to the separated protein subunits and fractions. Sera of two patients showed strong binding of omega-gliadins, while alpha-gliadins and LMW glutenin subunits of MW = 43 and 45 kDa were highly allergenic for two other subjects in the test group of patients.
醇溶蛋白和谷蛋白——小麦面筋的主要成分——是小麦籽粒中高度复杂且具有多态性的蛋白质。它们也是引发一系列食物过敏的过敏原蛋白。我们推测,化学结构和性质的多样性可能与面筋蛋白不同亚基和组分的免疫反应特性的多样化有关。在本研究中,我们使用从表现出不同小麦过敏症状的患者身上获得的IgE血清进行免疫印迹分析,以证明IgE抗体与通过SDS-PAGE分离的单个醇溶蛋白和谷蛋白之间免疫反应的特异性。结果表明,患者对分离出的蛋白质亚基和组分具有不同的IgE结合特征。两名患者的血清显示出与ω-醇溶蛋白的强结合,而在患者测试组中,α-醇溶蛋白以及分子量为43和45 kDa的低分子量谷蛋白亚基对另外两名受试者具有高度致敏性。