Dessi M, De Vincenzi M, Maialetti F, Mancini E
Laboratorio di Metabolismo e Biochimica Patologica, Istituto Superiore di Sanità, Roma, Italy.
Ital J Gastroenterol. 1992 Sep;24(7):397-9.
Previous studies suggested that the proteins and peptides that are responsible for coeliac small intestinal lesions, are also able to agglutinate K562(S) cells. On the contrary, peptides from whole gliadins from durum (tetraploid) wheat do not agglutinate these cells. Bread wheat alpha-gliadins have been identified as a major toxic fraction in coeliac disease. In the present research, alpha-gliadins were purified from durum and bread wheat cultivars. alpha-gliadin peptides from bread wheat were active in agglutinating K562(S) cells, whereas alpha-gliadin from durum wheat failed to induce any agglutinating activity. These results suggest that the lack of toxicity of gliadin from durum wheat cultivars is not related to a low content of alpha-gliadins but is mainly due to intrinsic structural differences from bread wheat gliadins.
先前的研究表明,导致乳糜泻小肠损伤的蛋白质和肽,也能够凝集K562(S)细胞。相反,来自硬粒(四倍体)小麦的全醇溶蛋白的肽不会凝集这些细胞。面包小麦α-醇溶蛋白已被确定为乳糜泻中的主要毒性成分。在本研究中,从硬粒小麦和面包小麦品种中纯化出α-醇溶蛋白。面包小麦的α-醇溶蛋白肽具有凝集K562(S)细胞的活性,而硬粒小麦的α-醇溶蛋白未能诱导任何凝集活性。这些结果表明,硬粒小麦品种醇溶蛋白缺乏毒性并非与α-醇溶蛋白含量低有关,而是主要由于其与面包小麦醇溶蛋白在内在结构上存在差异。