Isolation of isoforms of mouse prion protein with PrP(SC)-like structural properties.
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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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.
Chang
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JY
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000494:pharmacology; D002942:Circular Dichroism; D019286:Endopeptidase K / Q000494:pharmacology; D007700:Kinetics; D008027:Light; D013058:Mass Spectrometry; D051379:Mice; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000648:ultrastructure; D010957:Plasmids; D018620:PrPSc Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D020033:Protein Isoforms / Q000737:chemistry / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D013053:Spectrophotometry; D014508:Urea / Q000737:chemistry
D010446:Peptide Fragments; D018620:PrPSc Proteins; D020033:Protein Isoforms; D014508:Urea; D002918:Chymotrypsin; D019286:Endopeptidase K