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• W2024580111 abstract "Bacterially-produced recombinant prion protein (rPrP) is a frequently used model system for the study of the properties of wild-type and mutant prion proteins by biochemical and biophysical approaches. A range of approaches have been developed for the purification and refolding of untagged rPrP expressed as inclusion bodies in Escherichia coli, including refolding by dialysis and simultaneous on-column purification and refolding. In order to perform a higher-throughput analysis of different rPrP proteins, an approach that produces highly pure rPrP with a minimum of purification steps and a high yield per liter of induced bacterial culture is desired. Here, we directly compare purification approaches for untagged bovine rPrP as adapted to rapid, small-scale formats useful for higher-throughput studies. An analysis of protein yield, purity, oxidation, and refolding revealed significant differences between preparative methods as adapted to the small-scale format, and based on these findings we provide recommendations for future purifications. We also describe the utility of a sensitive commercial kit for thiol analysis of these preparations, the pH dependence of dimer formation during refolding of bovine rPrP, and bovine rPrP binding to cobalt affinity resin." @default.
• W2024580111 created "2016-06-24" @default.
• W2024580111 creator A5035716492 @default.
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• W2024580111 date "2012-04-01" @default.
• W2024580111 modified "2023-10-14" @default.
• W2024580111 title "A comparative analysis of rapid methods for purification and refolding of recombinant bovine prion protein" @default.
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• W2024580111 doi "https://doi.org/10.1016/j.pep.2012.02.008" @default.
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