Isolation of Isoforms of Mouse Prion Protein with PrPSC-like Structural Properties
- 12 October 2001
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 40 (44) , 13390-13396
- https://doi.org/10.1021/bi011111t
Abstract
Three novel conformational isomers of mouse prion protein mPrP(23−231) were prepared by incubating the reduced mPrP(23−231) in the presence of urea at mild acidic conditions. They are stable isomers that can be separated and isolated by reversed phase HPLC. These isomers, designated mPrP-a, mPrP-b, and mPrP-c, all exist in reduced state and monomeric form. They all exhibit a high content of β-sheet structure upon oligomerization at near-neutral pH. They are also partially resistant to proteolysis by proteinase K and chymotrypsin. These structural properties are hallmarks of pathogenic prion protein (PrPSC).Keywords
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