Number of the records: 1
Production, purification and oxidative folding of the mouse recombinant prion protein
- 1.0087156 - ÚOCHB 2008 RIV CZ eng J - Journal Article
Pavlíček, A. - Bednárová, Lucie - Holada, K.
Production, purification and oxidative folding of the mouse recombinant prion protein.
[Produkce, purifikace a oxidatinvní folding myšího recombinantního prionového proteinu.]
Folia Microbiologica. Roč. 52, č. 4 (2007), s. 391-397. ISSN 0015-5632. E-ISSN 1874-9356
R&D Projects: GA ČR GD310/05/H533
Grant - others:GA ČR(CZ) GA310/04/0419
Institutional research plan: CEZ:AV0Z40550506
Keywords : recombinant prion protein * production * purification * folding
Subject RIV: CE - Biochemistry
Impact factor: 0.989, year: 2007
http://www.biomed.cas.cz/mbu/folia/
The 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.
V práci je popsána exprese myšího prionového proteinu v cytoplazmě E.coli a jeho purifikace. Strukturální vlastnosti proteinu byly studovány pomocí spektroskopie cirkulárního dichroismu, resistence na stěpení proteinázou K a pomocí centrifugace v cukrózovém gradientu.
Permanent Link: http://hdl.handle.net/11104/0149077
Number of the records: 1