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Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Expression and purification of full-length recombinant PrP of high purity
Natallia Makarava1, Ilia V Baskakov
1Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD, USA.
Methods in Molecular Biology (Clifton, N.J.)
|June 26, 2008
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.
