Gliadin proteins of two winter wheat genotypes (the cultivar Ostka strzelecka and the line 60A) were analysed by ELISA using serum with a high content of IgE antibodies to gluten, obtained from patients showing symptoms of food and skin allergies. These wheats differed strongly in gliadin composition and gluten rheological properties. Two extraction methods were employed: a single-step method using 70% ethanol and a two-step method using 0.01 mol/L NaCl followed by 70% ethanol. ELISA results for Ostka strzelecka were much higher than those for line 60A at high antigen concentrations (dilutions 1:10 and 1:100); at lower antigen concentrations (dilutions 1:10.000 and 1:100.000), however, the opposite was observed. We also found that proteins extracted using the two-step method bound IgE antibodies much more strongly than those from the single-step extraction. This suggests that gliadin epitopes may be blocked by albumins and globulins that weaken the binding of IgE antibodies.