IMMUNOLOGICAL DIFFERENTIATION OF VARIOUS GLIADINS AND LOW M(R) SUBUNITS OF GLUTENIN USING ANTIPEPTIDE ANTISERA

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 Mr 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 Mr 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. © 1994 Academic Press Limited.