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- W2069776774 abstract "Mature prion protein (PrP) is a 208-residue polypeptide that contains a single disulfide bond. We report an alternative method to purify recombinant mouse PrP produced in Escherichia coli. Bacterial inclusion bodies were solubilized in a buffer containing 2 M urea at pH 12.5. The solubilized protein was rapidly purified on a nickel affinity column without a chaotrope gradient, followed by ion-exchange chromatography. The yield and purity of PrP produced by this alternative approach was similar to that obtained using a conventional solubilization and on-column refolding protocol. Recombinant PrP produced using the non-reducing purification protocol is properly folded, as determined by circular dichroism, and a competent substrate for amyloid fibril formation, as determined by Thoflavin-T dye binding assays. In summary, this report describes a rapid method for producing properly folded recombinant PrP without reducing agents or a chaotrope gradient." @default.
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- W2069776774 date "2012-01-01" @default.
- W2069776774 modified "2023-09-24" @default.
- W2069776774 title "NON-REDUCING ALKALINE SOLUBILIZATION AND RAPID ON-COLUMN REFOLDING OF RECOMBINANT PRION PROTEIN" @default.
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- W2069776774 doi "https://doi.org/10.1080/10826068.2011.564256" @default.
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