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Digested Ara h 1 has sensitizing capacity in Brown Norway rats
Summary Background Food allergies are a public health issue of growing concern, with peanuts in particular being associated with severe reactions. The peanut allergen, Ara h 1, belongs to the cupin plant food allergen family, which, unlike other structural families, appears to be broken down rapidly...
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Published in: | Clinical and experimental allergy 2009-10, Vol.39 (10), p.1611-1621 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Background
Food allergies are a public health issue of growing concern, with peanuts in particular being associated with severe reactions. The peanut allergen, Ara h 1, belongs to the cupin plant food allergen family, which, unlike other structural families, appears to be broken down rapidly following gastrointestinal digestion.
Objective
Using Ara h 1 as a model allergen, the ability of digested protein to sensitize has been investigated.
Methods
Ara h 1 was purified from whole roasted peanuts. Intact Ara h 1 was digested in an in vitro model, simulating the human gastrointestinal digestion process. Digestion products were analysed for peptide sizes and their ability to aggregate. Brown Norway (BN) rats, used as an animal model, were immunized with purified intact Ara h 1 or the gastrointestinal digestion products thereof. The sensitizing capacity was evaluated by analyses of specific antibody (IgG1, IgG2a and IgE) responses and ability to trigger mediator release of rat basophilic leukaemia (RBL)‐2H3 cells.
Results
The present study showed that Ara h 1 was broken down, resulting in peptide fragments of sizes |
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ISSN: | 0954-7894 1365-2222 |
DOI: | 10.1111/j.1365-2222.2009.03333.x |