Allergenicity of hen's egg-white proteins: IgE binding of native and deglycosylated ovomucoid

被引:26
作者
Besler, M [1 ]
Steinhart, H [1 ]
Paschke, A [1 ]
机构
[1] Univ Hamburg, Inst Biochem & Food Chem, D-20146 Hamburg, Germany
关键词
food allergy; egg-white; ovomucoid; deglycosylation; IgE binding; SDS-PAGE immunoblot; EAST inhibition; MALDI-TOF; CZE;
D O I
10.1080/09540109709354958
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Ovomucoid (OM) is a major allergen of hen's egg-white. Carbohydrate moieties from the glycoprotein were removed by chemical deglycosylation. Deglycosylated ovomucoid (d-OM) consists of five isoforms with molecular weights (MW) between 20.7 and 21.5 kDa whereas native OM has a MW of 28 kDa as determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. The IgE-binding properties of both proteins were investigated All patients' sera tested, showed strong IgE binding to both native OM and d-OM in SDS-PAGE/immunoblot. In enzyme-allergosorbent test experiments, 50% inhibition of IgE binding was observed at almost the same inhibitor concentrations of 67 and 57 ng ml(-1) for native OM and d-OM respectively. Results indicate that only epitopes on the protein backbone are responsible for IgE binding while carbohydrate residues do not participate in allergenic structures of OM.
引用
收藏
页码:277 / 288
页数:12
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