De Vincenzi M, Luchetti R, Peruffo A D, Curioni A, Pogna N E, Gasbarrini G
Laboratorio di Metabolismo e Biochimica Patologica, Istituto Superiore di Sanità, Roma, Italy.
J Biochem Toxicol. 1996;11(4):205-10. doi: 10.1002/(SICI)1522-7146(1996)11:4<205::AID-JBT7>3.0.CO;2-O.
Acetic-acid-soluble storage proteins from gluten of the bread wheat cv. Sprint 3 were fractionated by adsorption chromatography on 2000 A controlled-pore glass (CPG) beads, and glutenin polymers with molecular mass higher than 10(7) Da and free from monomeric gliadins were recovered. The glutenin polymers were found to consist of high-molecular-weight (HMW) and low-molecular-weight (LMW) glutenin subunits. Peptic-tryptic (PT) digests of glutenins were examined for their agglutination activity on human myelogenous leukemia K 562(S) cells, agglutination being strongly correlated with toxicity for the celiac intestine. The peptide fraction at a concentration of 1 g/L of culture medium was able to agglutinate 30% of K 562(S) cells, suggesting a moderate toxic effect. This toxicity may be accounted for by homologies in amino acid sequences between glutenin subunits and alpha/beta- and gamma-gliadins.
对面包小麦品种Sprint 3面筋中的乙酸可溶贮藏蛋白，采用在2000 Å可控孔径玻璃（CPG）微珠上进行吸附色谱法进行分级分离，回收了分子量高于10⁷ Da且不含单体麦醇溶蛋白的谷蛋白聚合物。发现谷蛋白聚合物由高分子量（HMW）和低分子量（LMW）谷蛋白亚基组成。检测了谷蛋白的胃蛋白酶-胰蛋白酶（PT）消化物对人髓性白血病K 562(S)细胞的凝集活性，凝集与对乳糜泻肠的毒性密切相关。浓度为1 g/L培养基的肽级分能够凝集30%的K 562(S)细胞，表明有中等毒性作用。这种毒性可能是由于谷蛋白亚基与α/β-和γ-麦醇溶蛋白之间氨基酸序列的同源性所致。
