Western immunoblotting of cereal proteins with monoclonal antibodies to wheat gliadin to investigate coeliac disease.

Western immunoblotting was used to investigate the binding of two monoclonal antibodies raised against unfractionated wheat gliadin to different cereal protein fractions separated by SDS-PAGE. Our results confirm the presence of considerable epitope sharing between the gliadin subfractions as well as barley and rye prolamins; however, there was less binding of these antibodies to bands present in oat avenins and maize zeins. The pattern of binding of one of these two antibodies to different cereal prolamins as well as to Frazer's fraction III corresponds closely to the known toxicity of these proteins to patients with coeliac disease.