Gliadins and glutenins--the main components of wheat gluten--are highly complex and polymorphic proteins of wheat kernels. They are also allergenic proteins causing a range of food allergies. We hypothesized that the diversity of chemical structures and properties may relate to the diversification of immunoreactive properties of various subunits and fractions of gluten proteins. In the present study we used IgE sera, obtained from patients manifesting different symptoms of wheat allergies, for immunobloting analysis, to prove the specificity of immunological reaction between IgE antibodies and individual gliadins and glutenins, separated by SDS-PAGE. The results suggest that patients have different characteristics of IgE binding to the separated protein subunits and fractions. Sera of two patients showed strong binding of omega-gliadins, while alpha-gliadins and LMW glutenin subunits of MW = 43 and 45 kDa were highly allergenic for two other subjects in the test group of patients.