Immunological Differentiation of Various Gliadins and Low Mr Subunits of Glutenin using Anti-peptide Antisera

Abstract Synthetic peptides conjugated to a protein carrier were used to immunise rabbits in an attempt to produce antisera specific for the different classes of gliadins and for the low M r glutenin subunits of wheat. Eight peptides were selected from regions of low homology situated in the N and C-terminal domains of these proteins. The anti-peptide antisera were assayed gliadin and glutenin fractions of the bread wheat Hardy by immunoblotting after SDS-PAGE separation and by ELISA. Six of the peptides, i.e. N-terminal peptides of α,β-type, γ-type and ω-type gliadins and low M r glutenin subunits and a C-terminal peptide of α,β-type gliadins, induced antibodies that reacted specifically with the cognate proteins. C-terminal peptides of γ-type gliadins induced antibodies that cross-reacted with ω-type gliadins.