| Literature DB >> 10646556 |
M De Vincenzi1, M Silano, R Luchetti, B Carratù, C Boniglia, N E Pogna.
Abstract
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.Entities:
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Year: 1999 PMID: 10646556 DOI: 10.1023/a:1008059519025
Source DB: PubMed Journal: Plant Foods Hum Nutr ISSN: 0921-9668 Impact factor: 3.921