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© Research
Publication : Molecular immunology

Conformational differences of human IgE on hydrophobic and hydrophilic solid phases detected by monoclonal antibodies

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular immunology - 01 Nov 1987

Anfosso F, Demeure C, Delaage M, Cheballah R, Bellot F, Bourgois A

Link to Pubmed [PMID] – 2447490

Mol. Immunol. 1987 Nov;24(11):1129-34

Very sensitive assays of IgE are required for determining prevalence of allergic reactions in children. In order to develop a sensitive two-site IRMA two kinds of mAb were produced. Antibodies specific for D epsilon 1 determinants were derived from immunization with a 40 kDa papain Fc fragment. They bound equally native and 56 degrees C heated IgE. D epsilon 2 specific mAb were obtained after immunization with IgE anti-D epsilon 1 complex and were selected on the basis of their inability to bind heated IgE. In a two-site assay on plastic plates, D epsilon 1 specific mAb led to the binding of IgE but always prevented further binding of anti-D epsilon 1 mAb, anti-human kappa chain mAb or allergen on bound IgE. This was not true when CNBr activated cellulose was used. The influence of the nature of the solid phase disappeared when D epsilon 2 specific mAb were coated on plastic tubes. In this case, the binding of a second mAb with identical or different fine specificity was observed. The best matched pair was E 164 (anti-D epsilon 2) on the solid phase and 6H10 (anti-D epsilon 1) as a tracer. As little as 0.2 UI/ml of IgE could be detected in a 2 hr test.

http://www.ncbi.nlm.nih.gov/pubmed/2447490