In vitro toxicity testing of alcohol-soluble proteins from diploid wheat Triticum monococcum in celiac disease.
Peptic-tryptic digests of alcohol-soluble proteins from flours of 10 accessions of Trificum monococcum with contrasting storage protein compositions and bread-making characteristics were found unable to agglutinate K562(S) cells even at a peptide concentration as high as 14 g/L, agglutination being strongly correlated with toxicity in celiac disease. When fractionated by affinity chromatography on Sepharose-6B coupled with mannan, peptic-tryptic digests separated into three fractions. Fraction C peptides were shown to agglutinate K562(S) cells, whereas peptides in fractions A and B and in the mixed fraction B + C were inactive, suggesting that fraction B contains "protective" peptides that interfere with toxic peptides in fraction C in their agglutinating activity. These results offer an opportunity to study the biochemical and genetic bases of wheat toxicity at the diploid level. Moreover, the reduced toxicity, if any, of Triticum monococcum in the celiac disease, along with the good grain characteristics of some "monococcum" accessions, greatly increases the economical prospects of this wheat species.
De Vincenzi
M
M
Laboratorio di Metabolismo e Biochimica Patologica, Istituto Superiore di Sanità, Rome, Italy.
Luchetti
R
R
Giovannini
C
C
Pogna
N E
NE
Saponaro
C
C
Galterio
G
G
Gasbarrini
G
G
D000371:Agglutination; D001939:Bread; D002446:Celiac Disease; D002448:Cell Adhesion / Q000187:drug effects; D002460:Cell Line; D002846:Chromatography, Affinity; D000431:Ethanol; D005433:Flour; D005903:Gliadin / Q000032:analysis; D006801:Humans; D010434:Pepsin A; D010446:Peptide Fragments / Q000302:isolation & purification / Q000633:toxicity*; D010940:Plant Proteins / Q000302:isolation & purification / Q000633:toxicity*; D014908:Triticum; D014357:Trypsin
D010446:Peptide Fragments; D010940:Plant Proteins; D000431:Ethanol; D005903:Gliadin; D014357:Trypsin; D010434:Pepsin A