抗原性
糖基化
化学
卵清蛋白
碳酸氢盐
免疫球蛋白E
碳酸氢钠
表位
碳酸钠
钠
生物化学
色谱法
抗体
抗原
免疫学
有机化学
受体
生物
作者
Xiaojuan Ma,Jinyan Gao,Hongbing Chen
摘要
Abstract BACKGROUND Ovalbumin ( OVA ) is a major allergen in hen egg. During thermal processing, reducing sugars contained in the hen egg white might easily undergo glycation with OVA , but few studies have been conducted on its corresponding immunoreactivity changes. The aim of the present study was to assess changes of the antigenicity, potential allergenicity and conformation of OVA after glycation in a wet‐thermal processing system under different concentrations of sodium carbonate–bicarbonate buffer . Results IgE binding of the glycated OVA was increased after glycation, and the higher the sodium carbonate–bicarbonate buffer concentration, the higher the IgE binding capacity. The increase in IgE binding of OVA corresponded well with the disruption of the disulfide bond, which exposed the epitopes initially buried. Antigenicity of the glycated OVA was increased, and the amount of the increase varied among samples treated under different buffer concentrations . Conclusion Glycation increased the allergenic potential for OVA , with the amount of increase varying with different sodium carbonate–bicarbonate buffer concentrations. © 2013 Society of Chemical Industry
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