timothy-grass/albumin

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Suppression of reaginic antibodies with modified allergens. III. Preparation of tolerogenic conjugates of common allergens with monomethoxypolyethylene glycols of different molecular weights by the mixed anhydride method.

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Our previous findings that antigens, such as ovalbumin (OA) and the extract of ragweed pollen (RAG), could be rendered nonantigenic, nonallergenic and tolerogenic by conjugation with polyethylene glycol (PEG) have been extended in the present study to the synthesis of conjugates of a variety of

The requirements for transferrin-dependent adherence of human granulocytes to pollen grains.

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Human granulocyte/pollen binding protein (GPBP), previously identified as serum transferrin, promoted prolonged firm adherence of neutrophils to Timothy grass pollen. Some characteristics of this adherence reaction are reported. GPBP-induced binding was time-, temperature- and

Immunization with purified natural and recombinant allergens induces mouse IgG1 antibodies that recognize similar epitopes as human IgE and inhibit the human IgE-allergen interaction and allergen-induced basophil degranulation.

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Molecular characterization of allergens by recombinant DNA technology has made rapid progress in the recent few years. In the present study we immunized mice with aluminum hydroxide-adsorbed purified recombinant major timothy grass pollen allergens (rPhl p 1, rPhl p 2, rPhl p 5), dog albumin, a

Nitration of pollen aeroallergens by nitrate ion in conditions simulating the liquid water phase of atmospheric particles.

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Pollen aeroallergens are present in atmospheric particulate matter (PM) where they can be found in coarse biological particles such as pollen grains (aerodynamic diameter dae>10μm), as well as fragments in the finest respirable particles (PM2.5; dae<2.5μm). Nitration of tyrosine residues in pollen

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