Expression and purification of full-length recombinant PrP of high purity

Natallia Makarava; Ilia V Baskakov

doi:10.1007/978-1-59745-234-2_10

Expression and purification of full-length recombinant PrP of high purity

Methods Mol Biol. 2008:459:131-43. doi: 10.1007/978-1-59745-234-2_10.

Authors

Natallia Makarava¹, Ilia V Baskakov

Affiliation

¹ Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA.

PMID: 18576153
DOI: 10.1007/978-1-59745-234-2_10

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.

MeSH terms

Animals
Bacteriolysis
Chromatography, High Pressure Liquid
Cricetinae
Escherichia coli / cytology
Imidazoles
Inclusion Bodies
Mesocricetus
Mice
PrPC Proteins / biosynthesis*
PrPC Proteins / isolation & purification*
PrPC Proteins / metabolism
Recombinant Proteins / biosynthesis*
Recombinant Proteins / isolation & purification*
Recombinant Proteins / metabolism
Transformation, Genetic

Substances

Imidazoles
PrPC Proteins
Recombinant Proteins
imidazoleacetic acid