IMMUNOAFFINITY ANALYSIS OF CROSS-REACTING ALLERGENS BY PROTEIN BLOTTING

IgE antibodies from sera having reactivity against ryegrass pollen pro tein allergens, wheat endosperm protein allergens and also several oth er cereal protein allergens were adsorbed with either ryegrass pollen or the wheat/globulin fraction immobilised on solid phases and subsequ ently eluted with low pH buffer. The eluted antibodies were reacted wi th sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE ) blots of the different allergens. Antibodies adsorbed and subsequent ly eluted from the two allergen sources recognised different spectra o f proteins in the ryegrass pollen and cereal allergen sources and indi cated the degree of immunological cross-reactivity. Intra-species cros s-reactivity of IgE antibodies was demonstrated employing similar meth ods to those used for the pollen and cereal allergens by using a recom binant allergen from the venom of the ant Myrmecia pilosula as the imm unoadsorbant protein on the solid phase.