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Purification and Recombinant Expression of Major Peanut Allergen Ara h 1
Authors:Zhihua Wu  Fei Yan  Xiaonan Wei  Xin Li  Ping Tong  Anshu Yang
Affiliation:1. State Key Laboratory of Food Science and Technology , Nanchang University , Nanchang , P.R. China;2. Sino-German Joint Research Institute , Nanchang University , Nanchang , P.R. China;3. Shandong Longda Bio-Products Co., Ltd , Yishui , P.R. China;4. State Key Laboratory of Food Science and Technology , Nanchang University , Nanchang , P.R. China;5. Sino-German Joint Research Institute , Nanchang University , Nanchang , P.R. China
Abstract: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. SDS-PAGE, 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.
Keywords:Ara h 1  expression  immunological analysis  MALDI-TOF MS  peanut  purification
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