Abstract
PrPC purification from cells and tissues requires high quantities of biological material, owing to the generally low cellular expression level of the protein [1,2]. Expression in E.coli circumvents this difficulty. It was used as a source of full-length prion protein as well as its (90-231) C-terminal fragment for biophysical and functional studies [3-9].
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Rezaei, H. (2004). Rapid Procedure for Purification and Renaturation of Recombinant PrP Protein. In: Lehmann, S., Grassi, J. (eds) Techniques in Prion Research. Methods and Tools in Biosciences and Medicine. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7949-1_4
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DOI: https://doi.org/10.1007/978-3-0348-7949-1_4
Publisher Name: Birkhäuser, Basel
Print ISBN: 978-3-7643-2224-3
Online ISBN: 978-3-0348-7949-1
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