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-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.
De Vincenzi
M
M
Laboratorio Alimenti, Istituto Superiore di Sanità, Rome, Italy.
Silano
M
M
Luchetti
R
R
Carratù
B
B
Boniglia
C
C
Pogna
N E
NE
D000371:Agglutination / Q000187:drug effects*; D000596:Amino Acids / Q000032:analysis; D002446:Celiac Disease / Q000378:metabolism*; D002846:Chromatography, Affinity; D004797:Enzyme-Linked Immunosorbent Assay; D005433:Flour; D010940:Plant Proteins / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D012639:Seeds / Q000737:chemistry*; D012995:Solubility
D000596:Amino Acids; D010940:Plant Proteins