Isolation of isoforms of mouse prion protein with PrP(SC)-like structural properties. |
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| Authors: | B Y Lu J Y Chang |
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| Institution: | Research Center for Protein Chemistry, Institute of Molecular Medicine, and the Department of Biochemistry and Molecular Biology, The University of Texas, Houston, Texas 77030, USA. |
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| 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 beta-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 (PrP(SC)). |
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