Immunoaffinity analysis of cross-reacting allergens by protein blotting.
IgE antibodies from sera having reactivity against ryegrass pollen protein allergens, wheat endosperm protein allergens and also several other cereal protein allergens were adsorbed with either ryegrass pollen or the wheat/globulin fraction immobilised on solid phases and subsequently eluted with low pH buffer. The eluted antibodies were reacted with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) blots of the different allergens. Antibodies adsorbed and subsequently eluted from the two allergen sources recognised different spectra of proteins in the ryegrass pollen and cereal allergen sources and indicated the degree of immunological cross-reactivity. Intra-species cross-reactivity of IgE antibodies was demonstrated employing similar methods to those used for the pollen and cereal allergens by using a recombinant allergen from the venom of the ant Myrmecia pilosula as the immunoadsorbent protein on the solid phase.
Donovan
G R
GR
Kolling Institute of Medical Research, Royal North Shore Hospital, St. Leonards, Australia.
Baldo
B A
BA
D000485:Allergens / Q000276:immunology*; D000918:Antibody Specificity; D002523:Edible Grain / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000097:blood / Q000276:immunology*; D007163:Immunosorbent Techniques; D008129:Lolium / Q000276:immunology; D011058:Pollen / Q000276:immunology; D011994:Recombinant Proteins / Q000276:immunology; D014908:Triticum / Q000276:immunology
D000485:Allergens; D011994:Recombinant Proteins; D007073:Immunoglobulin E