NR AHOF
AU Lu,B.Y.; Chang,J.Y.
TI Isolation of isoforms of mouse prion protein with PrPsc-like structural properties
QU Biochemistry 2001 Nov 6; 40(44): 13390-6
PT journal article
AB 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 (PrPsc).
MH Animal; Chromatography, High Pressure Liquid; Chymotrypsin/pharmacology; Circular Dichroism; Endopeptidase K/pharmacology; Kinetics; Light; Mice; Molecular Weight; Oxidation-Reduction; Peptide Fragments/chemistry/genetics/ultrastructure; Plasmids; PrPsc Proteins/*chemistry/*isolation & purification; Protein Conformation; Protein Denaturation; Protein Folding; Protein Isoforms/chemistry/isolation & purification; Protein Structure, Secondary; Spectrophotometry; Spectrum Analysis, Mass; Support, Non-U.S. Gov't; Urea/chemistry
AD 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
SP englisch
PO USA