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  • Title: Measurement of gluten using a monoclonal antibody to a sequenced peptide of alpha-gliadin from the coeliac-activating domain I.
    Author: Ellis HJ, Doyle AP, Wieser H, Sturgess RP, Day P, Ciclitira PJ.
    Journal: J Biochem Biophys Methods; 1994 Jan; 28(1):77-82. PubMed ID: 7512105.
    Abstract:
    A monoclonal antibody, raised against a sequenced 54 amino-acid peptide from the coeliac-activating N-terminal region of alpha-gliadin, was used in an assay for the measurement of gluten in foods. A double-sandwich ELISA using a polyclonal capture antibody produced standard curves for unfractionated gliadin and its alpha, beta, gamma and omega subfractions, and for rye, barley and oat prolamins. The sensitivity of the assay for unfractionated gliadin and rye prolamins was 15 ng/ml, for barley and oat prolamins 125 and 250 ng/ml, respectively. Prolamins from coeliac non-toxic rice, maize, millet and sorghum did not cross-react in the assay.
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