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

• Published in: Plant foods for human nutrition (Dordrecht) Vol. 54; no. 2; pp. 93 - 100
• Main Authors: Vincenzi, M. De (Istituto Superiore di Sanita, Rome (Italy). Lab. Alimenti), Silano, M, Luchetti, R, Carratu, B, Boniglia, C, Pogna, N.E
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 1999
• Subjects: ACIDE AMINE; Agglutination - drug effects; AGGLUTINATION TESTS; AMINO ACIDS; Amino Acids - analysis; AMINOACIDOS; Biological and medical sciences; Celiac Disease - metabolism; Cereal and baking product industries; CHENOPODIUM QUINOA; Chromatography, Affinity; Enzyme-Linked Immunosorbent Assay; FARINE NON CEREALIERE; Flour; Food industries; Fundamental and applied biological sciences. Psychology; GRAINE; HARINAS DE NO CEREAL; METABOLIC DISORDERS; NONCEREAL FLOURS; Plant Proteins - analysis; Plant Proteins - isolation & purification; Plant Proteins - pharmacology; PROLAMINAS; PROLAMINE; PROLAMINES; REACCIONES DE AGLUTINACION; REACTION D'AGGLUTINATION; SEEDS; Seeds - chemistry; SEMILLA; Solubility; TRASTORNOS METABOLICOS; TROUBLE DU METABOLISME; Peptides; Property composition relationship; Pepsin A; Coeliac disease; Cereal flour; Affinity chromatography; Pseudocereals; Dicotyledones; Angiospermae; Separation process; Aspartic endopeptidases; Agglutination; Alcoholic solution; Cell; Chenopodium quinoa; Human; Cytotoxic factor; Serine endopeptidases; Enzyme; Extraction process; Solubility; Chenopodiaceae; Peptidases; Trypsin; Vegetable crop; Aminoacid; Disease of the small intestine; Plant protein; Enzymatic digestion; Digestive diseases; Hydrolases; Spermatophyta; Prolamin; ELISA assay; Physicochemical properties
• ISSN: 0921-9668; 1573-9104
• DOI: 10.1023/A:1008059519025

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.