A peptide B3144, derived after peptic tryptic digestion of α-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 μg/ml for unfractionated wheat gliadin and rye prolamins, and 5 μg/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 α-gliadins in malted barley, suggesting t
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