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.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 351691
Title Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer
Author(s) Boxtel, E.L. van; Beers, M.M.C. van; Koppelman, S.J.; Broek, L.A.M. van den; Gruppen, H.
Source Journal of Agricultural and Food Chemistry 54 (2006)19. - ISSN 0021-8561 - p. 7180 - 7186.
Department(s) Food Chemistry
Publication type Refereed Article in a scientific journal
Publication year 2006
Keyword(s) ige-binding epitopes - ara-h-i - atopic-dermatitis - storage proteins - circular-dichroism - beta-conglycinin - food allergens - identification - hypersensitivity - superfamily
Abstract Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.
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