Allergen Ara h 1 Occurs in Peanuts as a Large Oligomer Rather Than as a Trimer

详细信息    查看全文

• 作者：Evelien L. van Boxtel ; Miranda M. C. van Beers ; Stef J. Koppelman ; Lambertus A. M. van den Broek ; Harry Gruppen
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2006
• 出版时间：September 20, 2006
• 年：2006
• 卷：54
• 期：19
• 页码：7180 - 7186
• 全文大小：315K
• 年卷期：v.54,no.19(September 20, 2006)
• ISSN：1520-5118

文摘

Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purificationof native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared toexist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure wasindependent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bringabout 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 ionicstrengths. The (partial) dissociation into trimers led to a change in the tertiary structure of themonomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compacttertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics areimportant for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 thanpreviously described.