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- W2121316618 abstract "RATIONALE: We have previously demonstrated the IgE binding capacity of the recombinant form of the soybean seed biotinylated protein (SBP). Here, we have purified the natural soybean and peanut SBPs and characterized their IgE reactivity. METHODS: Protein extracts were prepared from mature soybean and peanut embryos, which contain larger amounts of SBP. Purifications were carried out under denaturing (urea) conditions using streptavidin-affinity chromatography. The identity of the purified proteins was examined by streptavidin-HRP detection and mass spectrometry analysis (LC-MS). IgE reactivity to both SBPs was investigated by IgE capture ELISA (SBP biotin detection) and Western blotting (after SDS-PAGE) using 29 peanut and soy positive sera. RESULTS: Affinity purification performed on either soybean or peanut embryonic extracts resulted in a preparation enriched (>70%) with a biotinylated protein of approximately 72-kDa. Each of these proteins was identified as the SBPs of their respective species by LC-MS. IgE reactivity by ELISA showed that more than 50% of the patient's sera recognized the soybean and peanut SBPs. However, by Western blots, this frequency decreased below 30% for both SBPs, suggesting the existence of conformational epitopes. Overall, more patients had IgE reactivity to SBP from soybean than peanut. CONCLUSIONS: We have demonstrated the allergenicity of the purified soybean and peanut SBPs. The serum study showed a higher prevalence of sensitization to the soybean SBP compared to peanut. Our study also suggests that the ubiquitous seed biotinylated proteins could represent a new family of allergens." @default.
- W2121316618 created "2016-06-24" @default.
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- W2121316618 date "2010-02-01" @default.
- W2121316618 modified "2023-09-27" @default.
- W2121316618 title "Allergenicity of the Soybean and Peanut Seed Biotinylated Proteins" @default.
- W2121316618 doi "https://doi.org/10.1016/j.jaci.2009.12.871" @default.
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