Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 326365
Title Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization.
Author(s) Koppelman, S.J.; Knol, E.F.; Vlooswijk, R.A.A.; Wensing, M.; Knulst, A.C.; Hefle, S.L.; Gruppen, H.; Piersma, S.R.
Source Allergy 58 (2003)11. - ISSN 0105-4538 - p. 1144 - 1151.
DOI https://doi.org/10.1034/j.1398-9995.2003.00259.x
Department(s) Food Chemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) ara-h-i - atopic-dermatitis - ige binding - identification - glycinin - proteins - sera - hypersensitivity - epitopes - cloning
Abstract Background: Peanut allergen Ara h 3 has been the subject of investigation for the last few years. The reported data strongly depend on recombinant Ara h 3, since a purification protocol for Ara h 3 from peanuts was not available. Methods: Peanut allergen Ara h 3 (glycinin), was purified and its posttranslational processing was investigated. Its allergenic properties were determined by studying IgE binding characteristics of the purified protein. Results: Ara h 3 consists of a series of polypeptides ranging from approximately 14 to 45 kDa that can be classified as acidic and basic subunits, similar to the subunit organization of soy glycinin. N-terminal sequences of the individual polypeptides were determined, and using the cDNA deduced amino-acid sequence, the organization into subunits was explained by revealing posttranslational processing of the different polypeptides. IgE-binding properties of Ara h 3 were investigated using direct elisa and Western blotting with sera from peanut-allergic individuals. The basic subunits, and to a lesser extent the acidic subunits, bind IgE and may act as allergenic peptides. Conclusions: We conclude that peanut-derived Ara h 3, in contrast to earlier reported recombinant Ara h 3, resembles, to a large extent, the molecular organization typical for proteins from the glycinin family. Furthermore, posttranslational processing of Ara h 3 affects the IgE-binding properties and is therefore an essential subject of study for research on the allergenicity of Ara h 3.
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