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- W2604724340 abstract "ABSTRACTIn this study, we produced the recombinant form of parvalbumin from wolf-herring fish and determined its IgE reactivity. Parvalbumin cDNA was sub-cloned into pET28 and expressed in Escherichia coli BL-21. The immunoreactivities of the recombinant and native parvalbumins were compared, and the effect of calcium binding was determined by sera from 25 fish-allergic patients. ELISA and Western blotting confirmed similar IgE-reactivities of the recombinant and native proteins and confirmed that this phenomenon is highly dependent on calcium binding. The recombinant protein was 94.5% similar to carp parvalbumin (Cyp c1). Approximately 72% of patients reacted strongly with recombinant parvalbumin, 80% of them reacted with the native form and only 56% showed IgE reactivity with crude extract. Because the IgE-binding capacity of recombinant wolf-herring parvalbumin is retained and is highly similar to Cyp c1, the wild and hypoallergenic forms of this allergen could be used for diagnosis and immunotherapy o..." @default.
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- W2604724340 date "2017-04-04" @default.
- W2604724340 modified "2023-10-16" @default.
- W2604724340 title "Expression of recombinant parvalbumin from wolf-herring fish and determination of its IgE-binding capability" @default.
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- W2604724340 doi "https://doi.org/10.1080/09540105.2017.1306493" @default.
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