INVIVO ALLERGENIC ACTIVITIES OF 11 PURIFIED MEMBERS OF A MAJOR ALLERGEN FAMILY FROM WHEAT AND BARLEY FLOUR

Eleven purified members of the alpha-amylase/trypsin inhibitor family from wheat and barley that showed very different IgE-binding capacitie s 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 sensitizatio n to wheat flour as verified by skin test, RAST and challenge test. Th e three members of the protein family with highest IgE binding in vitr o (the glycosylated subunits of tetrameric alpha-amylase inhibitors CM 16 from wheat and CMb* from barley, and the barley monomeric inhibito r BMAI-1) were found to be the strongest allergens as indicated by ski n sensitivity in prick tests.