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In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method 被引量:1

In Vitro Refolding Process of Bovine Allergen β-lactoglobulin by Multispectroscopic Method
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摘要 Objective To characterize the relationship between the refolding process of recombinant bovine β-1actoglobulin and its immunoreactivity for clinical purposes. To establish a spectral method which examine the extent of recombinant allergen renaturation. Methods The refolding process of recombinant bovine β-1actoglobulin was investigated by using circular dichroism, fluorescence and synchronous fluorescence spectra. IgE-binding capacity of recombinant protein was analyzed by ELISA. In addition, bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro. Results Renaturation of recombinant bovine β-1actoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity. Conclusion The degree of protein renaturation Results from this study may be of help for food future. correlated with the IgE-binding capacity of the protein. allergy therapy and development of vaccination in the Objective To characterize the relationship between the refolding process of recombinant bovine β-1actoglobulin and its immunoreactivity for clinical purposes. To establish a spectral method which examine the extent of recombinant allergen renaturation. Methods The refolding process of recombinant bovine β-1actoglobulin was investigated by using circular dichroism, fluorescence and synchronous fluorescence spectra. IgE-binding capacity of recombinant protein was analyzed by ELISA. In addition, bioinformatic methods were used to explain the spectral characteristics and analyze the relationship between the conformational changes and the immunoreactivity of the protein during renaturation in vitro. Results Renaturation of recombinant bovine β-1actoglobulin resulted in a more compact structure resembling the natural counterpart with stronger IgE-binding capacity. Conclusion The degree of protein renaturation Results from this study may be of help for food future. correlated with the IgE-binding capacity of the protein. allergy therapy and development of vaccination in the
出处 《Biomedical and Environmental Sciences》 SCIE CAS CSCD 2012年第3期334-339,共6页 生物医学与环境科学(英文版)
基金 supported by the Natural Science Foundation of China (30871752) the High-tech Industrialization Funding of Guangdong Province (2009B011300010)
关键词 Food allergen Β-LACTOGLOBULIN Protein folding SPECTROSCOPY IMMUNOREACTIVITY Food allergen β-Lactoglobulin Protein folding Spectroscopy Immunoreactivity
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