The allergenic determinants of this protein were identified by SDS-PAGE and immunoblot after CNBr treatment.Īmong Ic fractions, Ic-VIII was highly potent by ELISA, skin tests and showed cross-reactivity with 4 other tropical grasses by immunoblot and ELISA inhibition. A 67-kD protein was purified to homogeneity from Ic-VIII. Allergenic activity of the fractions was checked by ELISA, skin tests, ELISA inhibition and immunoblot using sera of Ic-sensitive patients. Ic pollen extract was fractionated using DEAE Sephadex A-50, Sephadex G-200 and Mono Q column. To isolate, purify and characterize a cross-reactive allergenic protein from Ic pollen extract for diagnosis and therapy of grass pollen allergy. Earlier studies have recognized Imperata cylindrica (Ic) pollen as an important source of aeroallergen which contained 7 IgE binding proteins in the MW range of 85-16 kD.
Grass pollens are known to induce type I allergic reactions in a large number of genetically predisposed individuals.
