Summary
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.
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© 2008 Humana Press, a part of Springer Science + Business Media, LLC
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Makarava, N., Baskakov, I.V. (2008). Expression and Purification of Full-Length Recombinant PrP of High Purity. In: Hill, A.F. (eds) Prion Protein Protocols. Methods in Molecular Biology™, vol 459. Humana Press. https://doi.org/10.1007/978-1-59745-234-2_10
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DOI: https://doi.org/10.1007/978-1-59745-234-2_10
Publisher Name: Humana Press
Print ISBN: 978-1-58829-897-3
Online ISBN: 978-1-59745-234-2
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