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

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    SYSNO ASEP0087156
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JOstatní články
    TitleProduction, purification and oxidative folding of the mouse recombinant prion protein
    TitleProdukce, purifikace a oxidatinvní folding myšího recombinantního prionového proteinu
    Author(s) Pavlíček, A. (CZ)
    Bednárová, Lucie (UOCHB-X) RID, ORCID
    Holada, K. (CZ)
    Source TitleFolia Microbiologica. - : Springer - ISSN 0015-5632
    Roč. 52, č. 4 (2007), s. 391-397
    Number of pages7 s.
    Languageeng - English
    CountryCZ - Czech Republic
    Keywordsrecombinant prion protein ; production ; purification ; folding
    Subject RIVCE - Biochemistry
    R&D ProjectsGD310/05/H533 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z40550506 - UOCHB-X (2005-2011)
    AnnotationThe method of overexpression of the full-length mouse recombinant prion protein in cytoplasm of E.coli and its effective purification is described. The folding state of the protein was studied using circular dichroism spectroscopy, by the resistance to cleavage by proteinase K and by centrifugation in suchrose gradient.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    Contactasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
    Year of Publishing2008
Number of the records: 1  

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