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In vivo allergenic activities of eleven purified members of a major allergen family from wheat and barley flour
Author(s) -
ARMENTIA A.,
SANCHEZMONGE R.,
GOMEZ L.,
BARBER D.,
SALCEDO G.
Publication year - 1993
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1993.tb00347.x
Subject(s) - allergen , in vivo , in vitro , trypsin inhibitor , immunoglobulin e , amylase , wheat flour , trypsin , food science , chemistry , allergy , biology , enzyme , immunology , biochemistry , microbiology and biotechnology , antibody
Summary Eleven purified members of the α‐amylase/trypsin inhibitor family from wheat and barlcy that showed very different IgE‐binding capacities when previously assayed in vitro . were used in double blind in vivo diagnostic tests to further evaluate their allergenic activity. These tests were carried out in 31 patients who showed allergic scnsilization to wheat flour as veritied by skin test, RAST and challenge test. The three members of the protein family with highest igl ; binding in vitro (the glycosylated subunits of tetrameric α‐amylase inhibitors CM16* from wheat and CMb* from barley, and the barley monomeric inhibitor BMAI‐1) were found to be the strongest allergens as indicated by‐skin sensitivity in prick tests.