Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1

This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, olig...

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Veröffentlicht in:Journal of agricultural and food chemistry 2008-03, Vol.56 (6), p.2223-2230
Hauptverfasser: van Boxtel, Evelien L, Koppelman, Stef J, van den Broek, Lambertus A. M, Gruppen, Harry
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Sprache:eng
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Zusammenfassung:This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, oligomeric Ara h 1, either unheated or preheated, was hydrolyzed by pepsin at a lower rate than trimeric Ara h 1. Peptides with relatively high molecular masses were shown to be able to bind IgE, whereas peptides with lower molecular masses (
ISSN:0021-8561
1520-5118
DOI:10.1021/jf072907n