title: Expression and purification of full-length recombinant PrP of high purity.
abstract: Certain applications in the prion field require recombinant prion protein (PrP) of high purity and quality. Here, we report an experimental procedure for expression and purification of full-length mammalian prion protein. This protocol has been proved to yield PrP of extremely high purity that lacks PrP adducts, which are normally generated as a result of spontaneous oxidation or degradation.
authors.affiliation: Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA.
authors.forename: Natallia
authors.initials: N
authors.lastname: Makarava
authors.forename: Ilia V
authors.initials: IV
authors.lastname: Baskakov
mesh_terms: D000818:Animals; D001433:Bacteriolysis; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D004926:Escherichia coli / Q000166:cytology; D007093:Imidazoles; D002479:Inclusion Bodies; D008647:Mesocricetus; D051379:Mice; D018621:PrPC Proteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification* / Q000378:metabolism; D014170:Transformation, Genetic
chemical_list: D007093:Imidazoles; D018621:PrPC Proteins; D011994:Recombinant Proteins; C005954:imidazoleacetic acid