The edible seeds of the quinoa plant contain small quantities of alcohol-soluble protein which, after peptic-tryptic digestion, are unable to agglutinate K562(s) cells. When separated by affinity chromatography on sepharose-6B coupled with mannan, peptic-tryptic digest separated in two fractions. Fraction B peptides (about 1% of total protein) were shown to agglutinate K562(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 contains protective peptides that interfere with the agglutinating activity of toxic peptides in fraction B.
CITATION STYLE
De Vincenzi, M., Silano, M., Luchetti, R., Carratù, B., Boniglia, C., & Pogna, N. E. (1999). Agglutinating activity of alcohol-soluble proteins from quinoa seed flour in celiac disease. Plant Foods for Human Nutrition, 54(2), 93–100. https://doi.org/10.1023/A:1008059519025
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