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首页> 外文期刊>Life sciences >HYDROPHOBIC INTERACTIONS BETWEEN GLIADIN AND PROTEINS AND CELIAC DISEASE
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HYDROPHOBIC INTERACTIONS BETWEEN GLIADIN AND PROTEINS AND CELIAC DISEASE

机译：胶质蛋白和蛋白质之间的疏水相互作用与宫颈疾病

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Gliadin-protein interaction and its relationship to the pathogenesis hypotheses of celiac disease was investigated. Wheat germ agglutinin was not immunodetected in gliadin preparations. Peptic-tryptic gliadin digest was used to study the gliadin-protein interactions by crossed immunoelectrophoresis and affinity blotting. Biotinylated gliadin digest interacted with IgG and bovine serum albumin but not with several glycoproteins. Since albumin and IgG light chains are not glycosylated, this interaction is not lectin-like, neither completely immunological because of recognition of the IgG Fc fraction. Immobilized and boiled IgG was not recognized by gliadin digest as a lectin. Gliadin digest fractions from T-gel chromatography reduced the fluorescence intensity of cis-parinaric acid bound to albumin. The gliadin-protein interaction is not lectin-like or completely immunological but hydrophobic. Hydrophobicity of gliadins may contribute to the pathogenic events that result in celiac disease. [References: 31]
机译：研究了醇溶蛋白与蛋白质的相互作用及其与乳糜泻发病假说的关系。在麦醇溶蛋白制剂中未免疫检测到小麦胚芽凝集素。消化-胰蛋白酶麦醇溶蛋白消化物通过交叉免疫电泳和亲和印迹来研究麦醇溶蛋白-蛋白质相互作用。生物素化的麦醇溶蛋白消化物与IgG和牛血清白蛋白相互作用，但不与几种糖蛋白相互作用。由于白蛋白和IgG轻链未糖基化，因此这种相互作用不是凝集素样的，由于对IgG Fc组分的识别，也不完全是免疫学的。麦醇溶蛋白消化不能将固定和煮沸的IgG识别为凝集素。来自T-凝胶色谱的麦醇溶蛋白消化级分降低了与白蛋白结合的顺式-头皮酸的荧光强度。麦醇溶蛋白与蛋白质的相互作用不是凝集素样或完全免疫学上的，而是疏水的。麦醇溶蛋白的疏水性可能导致导致乳糜泻的致病性事件。 [参考：31]

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