• 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