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Folia Microbiol (Praha). 2007;52(4):391-7.

Production, purification and oxidative folding of the mouse recombinant prion protein.

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Institute of Microbiology and Immunology, 1st Faculty of Medicine, Charles University, 128 00 Prague, Czechia.


The method leading to overexpression of the full-length mouse recombinant prion protein (mrPrP 23-231) in the cytoplasm of E. coli as a his-PrP fusion protein and its effective purification using affinity chromatography is described. A typical yield of the method was 8-10 mg his-mrPrP per L of the bacterial culture. The purity of purified protein was > 95 %. The purified his-mrPrP was converted to a soluble form and its folding to alpha-helical and beta-sheet conformations was studied. The properties of differently folded mrPrP were determined by measuring their circular dichroism spectra, partial resistance to cleavage by proteinase K and by centrifugation in sucrose gradient.

[Indexed for MEDLINE]

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