Recombinant Prion Protein Purification

Syrian hamster recombinant prion protein (rHaPrP90-231) was prepared according to published protocol^{8 (link)}. Shortly, inclusion bodies produced by E. coli were solubilized in 8 M guanidine HCl and the protein purified using chromatography on Ni-Sepharose™ 6 Fast Flow (Cytiva). The rHaPrP90-231 was refolded on the column, eluted with a gradient of imidazole and dialyzed^{16 (link)}. The protein absorbance was measured and 0.22 μm filtered aliquots stored at – 80 °C.

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Baranová S., Moško T., Brůžová M., Haldiman T., Kim C., Safar J.G., Matěj R, & Holada K. (2024). Detection of prions in matching post-mortem skin and cerebrospinal fluid samples using second-generation real-time quaking-induced conversion assay. Scientific Reports, 14, 6294.

Publication 2024

Ni-Sepharose™ 6 Fast Flow

Corresponding Organization :

Other organizations : Charles University, Thomayer University Hospital, Case Western Reserve University, University School

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Variable analysis

independent variables

Preparation of Syrian hamster recombinant prion protein (rHaPrP90-231) according to published protocol

dependent variables

Protein absorbance

control variables

Inclusion bodies produced by E. coli
Solubilization of inclusion bodies in 8 M guanidine HCl
Purification using Ni-Sepharose™ 6 Fast Flow chromatography
Refolding of rHaPrP90-231 on the column
Elution with a gradient of imidazole
Dialysis of the protein
0.22 μm filtration of aliquots
Storage of the protein at -80 °C

controls

No positive or negative controls were explicitly mentioned.

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