Demonstration of the presence of coeliac-activating gliadin-like epitopes in malted barley.
A peptide B3144, derived after peptic tryptic digestion of alpha-gliadin and corresponding to residues 3-56 from the coeliac-activating domain I, was previously used to produce monoclonal antibodies. A dot immunobinding assay was developed using these antibodies to detect gluten in wheat, rye, barley and oats. The limit of sensitivity of the assay was 1 microgram/ml for unfractionated wheat gliadin and rye prolamins, and 5 micrograms/ml for barley and oat prolamins. Extracts of flours from coeliac non-toxic rice, maize, millet and sorghum gave negative results. Malt, which represents a partial hydrolysate of barley prolamins, was shown to contain the equivalent of 100-200 mg of barley prolamins/100 g of malt. The assay demonstrates the presence of intact epitopes from the coeliac-activating domain I of alpha-gliadins in malted barley, suggesting toxicity.
Ellis
H J
HJ
Rayne Institute, St. Thomas' Hospital, London, UK.
Doyle
A P
AP
Day
P
P
Wieser
H
H
Ciclitira
P J
PJ
D002446:Celiac Disease / Q000276:immunology*; D003429:Cross Reactions; D002523:Edible Grain / Q000276:immunology; D000939:Epitopes / Q000302:isolation & purification*; D005903:Gliadin / Q000276:immunology*; D001467:Hordeum / Q000276:immunology*; D006801:Humans; D015151:Immunoblotting
D000939:Epitopes; D005903:Gliadin