Characterization of Dac g 4, a major basic allergen from Dactylis glomerata pollen.

Monoclonal antibodies were produced against Dac g 4, a purified major basic allergen from Dactylis glomerata pollen. Their ability to be used for immunopurification of Dac g 4 was studied on a BIAcore apparatus (Pharmacia). The allergen was purified by affinity chromatography with one monoclonal antibody.

Cloning, sequencing and immunological characterization of Dac g 3, a major allergen from Dactylis glomerata pollen.

Preliminary work showed that a 14-kDa allergen with a pI of 9 was recognized by more than 60% of sera from Dactylis glomerata (Dac g) pollen-allergic individuals. The N-terminal amino acid sequence of this Dac g allergen was determined by Edman degradation and compared with that of Lol p 3, a major allergen of Lolium perenne. A sequence identity of 65% was found, suggesting that the Dac g allergen could be the homologue of Lol p 3 and therefore named Dac g 3.

Comparison of three horizontal two-dimensional electrophoretic techniques to separate grass pollen allergens.

The identification and characterization of allergenic components are important for improving both diagnosis and therapy of allergy. We have studied grass pollen crude extract for better characterization of the allergen repertoire recognized by allergic patient IgE antibodies. Two-dimensional electrophoresis are the methods of choice to define physico-chemical characteristics of the allergens as they give isoelectric points and molecular mass of the analyzed samples.