Expression and purification of full-length recombinant PrP of high purity.
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.
Makarava
Natallia
N
Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA.
Baskakov
Ilia V
IV
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
D007093:Imidazoles; D018621:PrPC Proteins; D011994:Recombinant Proteins; C005954:imidazoleacetic acid