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Title: Quantitation of IgE antibody specific for ragweed and grass allergens: binding of radiolabeled allergens by solid-phase bond IgE

Journal Article · · J. Allergy Clin. Immunol.; (United States)

IgE antibody specific for multiple allergens extracted from grass and ragweed pollens was measured by radioimmunoassay. The assay depends on the interaction between IgE antibody bound to a polystyrene solid phase, /sup 125/I-labeled grass allergens (GA), and ragweed allergens (RW). The binding of /sup 125/I RW by serum IgE antibody from 37 allergic patients ranged from 0.2 ng to 75 ng RW protein (P) bound per ml. This binding of /sup 125/I RW by patient's IgE was paralleled by their IgE binding of /sup 125/I antigen E (AgE), a purified allergen from ragweed pollen (r = 0.90, p less than 0.001). Inhibition of patient's IgE binding of /sup 125/I RW by highly purified AgE ranged from 25 to 85% indicated individual differences in patient's IgE response to inhaled ragweed pollen. The binding of /sup 125/I GA by serum IgE antibody from 7 grass-sensitive patients ranged from 0.6 ng GA P bound per ml to 15 ng. This assay should be useful in the study of IgE responses to environmental agents containing multiple allergens and has the advantage that other antibody classes cannot interfere with the interaction between IgE antibody and labeled allergens.

Research Organization:
Northwestern Univ., Chicago, IL
OSTI ID:
6741568
Journal Information:
J. Allergy Clin. Immunol.; (United States), Vol. 62:2
Country of Publication:
United States
Language:
English