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  • Title: Purification and characterization of the major allergen from apple and its allergenic cross-reactivity with Bet v 1.
    Author: Fahlbusch B, Rudeschko O, Müller WD, Schlenvoigt G, Vettermann S, Jäger L.
    Journal: Int Arch Allergy Immunol; 1995 Oct; 108(2):119-26. PubMed ID: 7549498.
    Abstract:
    The major allergen from apple extract was concentrated by anion exchange chromatography and further purified by reverse-phase HPLC. A distinct peak with a high degree of homogeneity was obtained. The isolated protein has a MW of 18 kD and specific IgE-binding capacity (immunoblotting, IgE-binding inhibition). N-terminal amino acid analyses of the allergen allowed 37 cleavages and showed 67.6% identity to Bet v 1, the major allergen of birch pollen. Enzyme immunoassay inhibition studies with serum of birch/apple-allergic patients showed that besides cross-reacting structures to Bet v 1, apple-specific IgE antibodies could exist. Monoclonal antibodies (mAbs) were raised against the 18-kD allergen from apple and characterized by means of immunoblotting and ELISA. Only three of the eight studied mAbs reacted with Bet v 1.
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