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Purification and Recombinant Expression of Major Peanut Allergen Ara h 1

文献类型： 外文期刊

作者： Wu, Zhihua 2 ; Yan, Fei 1 ; Wei, Xiaonan 1 ; Li, Xin 1 ; Tong, Ping 1 ; Yang, Anshu 2 ; Tang, Ronghua 4 ; Chen, Hongbing 1 ;

作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Peoples R China

2.Nanchang Univ, Sino German Joint Res Inst, Nanchang 330047, Peoples R China

3.Shandong Longda Bioprod Co Ltd, Yishui, Peoples R China

4.Guangxi Acad Agr Sci, Cash Crops Res Inst, Nanning 530007, Peoples R China

关键词： Ara h 1;expression;immunological analysis;MALDI-TOF MS;peanut;purification

期刊名称：PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY （ 影响因子：2.162； 五年影响因子：1.901 ）

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收录情况： SCI

摘要： Reaction to peanut, as one of the major food allergens, has become an increasingly common life-threatening disorder. Although peanut allergens have been extensively identified, Ara h 1 is still too expensive to be applied in food safety or clinical utility. In this study, the purification, expression, and immunological analyses of Ara h 1 are investigated. It was shown that a high purity (>95%) of Ara h 1 could be prepared by either purification or expression. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Western blot, and mass spectroscopy were used to identify the Ara h 1, and it was found that natural Ara h 1 (nAra h 1) and expressed Ara h 1 (rAra h 1) have the same properties, including amino acid sequence. In particular, rAra h 1 reacted positively with anti-nAra h 1 serum, showing their similar immunological property. Thus, by either purification or expression, Ara h 1 could be prepared with low cost, as performed in the present work. SDSPAGE, mag trix-assisted laser desorption/ionization time-of-flight mass spectroscopy (MALDI-TOF MS), and immunological analysis confirmed that both forms of Ara h 1 had the same properties.

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