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Characterization and stability of specific IgE to white egg's, gliadin's and peanut's proteins among children. | LitMetric

Characterization and stability of specific IgE to white egg's, gliadin's and peanut's proteins among children.

Iran J Allergy Asthma Immunol

Laboratory of Bioactive Molecules (LMBSF), Faculty of Sciences and Technology, Fez, Morocco.

Published: June 2010

The aim of the present study was to characterize allergen-specific immunoglobulin E (IgE) among children in Fez region. Eighty one children were recruited from the Hospital University Center of Fez. All of them had completed a questionnaire before taking sera. The sera were used to measure total IgE and specific data to proteins of egg's white (EWP), peanuts (PP) and gliadins (G). In last part, we studied the reactivity of specific IgE to native and to heat- and acid-treated allergens. Allergen-specific IgE measurement indicated more positive values for gliadins (46.9% up to 2IU/ml) than egg white's (29.6%) and peanut's proteins (22.2%). According to predictive values published by Sampson (2001), 14.3% of children are sensitive to egg white's proteins, 4.1% to gliadins and 2.7% to peanut's proteins. The allergenic potential of EWP and gliadins among children were partially diminished by heat and acid treatment. Allergen-specific IgE measurement indicates that children from Fez region are more sensitive to EWP than peanut's proteins and gliadins. Treatments of these food proteins indicated that recognition by children IgE can be reduced by thermal or acid treatment of these allergens.

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