Production, purification and oxidative folding of the mouse recombinant prion protein
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18062188
DOI
10.1007/bf02932094
Knihovny.cz E-zdroje
- MeSH
- chromatografie afinitní MeSH
- cirkulární dichroismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- Escherichia coli genetika metabolismus MeSH
- myši MeSH
- oxidace-redukce MeSH
- peptidové fragmenty biosyntéza chemie genetika izolace a purifikace MeSH
- priony biosyntéza chemie genetika izolace a purifikace MeSH
- rekombinantní proteiny biosyntéza chemie genetika izolace a purifikace MeSH
- sbalování proteinů MeSH
- western blotting MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- peptidové fragmenty MeSH
- prion protein (23-231) MeSH Prohlížeč
- priony MeSH
- rekombinantní proteiny MeSH
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.
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