Title of article
Vicilin and the basic subunit of legumin are putative chickpea allergens
Author/Authors
Bar-El Dadon، نويسنده , , Shimrit and Pascual، نويسنده , , Cristina Yolanda and Eshel، نويسنده , , Dani and Teper-Bamnolker، نويسنده , , Paula and Paloma Ibلٌez، نويسنده , , Marيa Dolores and Reifen، نويسنده , , Ram، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2013
Pages
6
From page
13
To page
18
Abstract
IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been characterized.
m pool from paediatric patients allergic to chickpeas was used to detect IgE-binding proteins from chickpea seeds by immunoassay and immunoblot inhibition assay. Protein samples enriched in chickpea legumin and vicilin were obtained by anion exchange chromatography, and were identified by mass spectrometric analysis.
munoassays of globulin fractions from chickpeas revealed that vicilin (50 kDa) and the basic subunit of legumin (20 kDa) were bound by IgE from patient sera. Pea and lentil protein extracts strongly inhibited the IgE binding to chickpea globulin.
culate that vicilin and the basic subunit of legumin are major chickpea allergens. Also, the globulin fraction of chickpea likely cross-reacts with the allergenic proteins of pea and lentil.
Keywords
chickpea , legumes , food allergy , Cross reactivity , IGE
Journal title
Food Chemistry
Serial Year
2013
Journal title
Food Chemistry
Record number
1971946
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