Agglutinating activity of alcohol-soluble proteins from quinoa seed flour in celiac disease

The edible seeds of the quinoa plant contain small quantities of alcohol-so luble protein which, after peptic-tryptic digestion, are unable to agglutin ate K562(s) cells. When separated by affinity chromatography on sepharose-6 B coupled with mannan, peptic-tryptic digest separated in two fractions. Fr action B peptides (about 1% of total protein) were shown to agglutinate K56 2(s) cells at a very low concentration, whereas peptides in fraction A and in the mixed fraction A+B were inactive, suggesting that fraction A contain s protective peptides that interfere with the agglutinating activity of tox ic peptides in fraction B.