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Pubmed ID :3138115
Publication Date : //

Purification and properties of the cellular and scrapie hamster prion proteins.


During scrapie infection an abnormal isoform of the prion protein (PrP), designated PrPSc, accumulates and is found to copurify with infectivity; to date, no nucleic acid has been found which is scrapie-specific. Both uninfected and scrapie-infected cells synthesize a PrP isoform, denoted PrPC, which exhibits physical properties that differentiate it from PrPSc. PrPC was purified by immunoaffinity chromatography using a PrP-specific monoclonal antibody cross-linked to protein-A--Avidgel. PrPSc was purified by detergent extraction, poly(ethylene glycol) precipitation and repeated differential centrifugation of PrPSc polymers. Both PrP isoforms were found to have the same N-terminal amino acid sequence which begins at a predicted signal peptide cleavage site. The first 8 residues of PrPC were found to be KKXPKPGG and the first 29 residues of PrPSc were found to be KKXPKPGGWNTGGSXYPGQGSPGGNRYPP. Arg residues 3 and 15 in PrPSc and 3 in PrPC appear to be modified since no detectable signals (denoted X) were found at these positions during gas-phase sequencing. Both PrP isoforms were found to contain an intramolecular disulfide bond, linking Cys 179 and 214, which creates a loop of 36 amino acids containing the two N-linked glycosylation sites. Development of a purification protocol for PrPC should facilitate comparisons of the two PrP isoforms and lead to an understanding of how PrPSc is synthesized either from PrPC or a precursor.

Authors : Turk E , Teplow D B , Hood L E , Prusiner S B ,

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PR-906 PrPc (globular domain, residues 90_231)His Prion Protein, cellular form hamster, recombinant, E. coli 50 µg
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PR-909 native PrPc (full length, residues 23_231)His Prion Protein, cellular form hamster, recombinant, E. coli 5 µg
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PR-906 Proteins: PrPc (globular domain, residues 90-231)His Prion Protein, cellular formhamster, recombinant, E. coli 50
PR-905 Proteins: PrPc (globular domain, residues 90-231)His Prion Protein, cellular formhuman, recombinant, E. coli 50
PR-904 Proteins: PrPc (full length, residues 23-230)His Prion Protein, cellular formmouse, recombinant, E. coli 50
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PR-902 Proteins: PrPc (full length, residues 23-231)His Prion Protein, cellular formhuman, recombinant, E. coli 50
PR-911 Proteins: native PrPc (globular domain, residues 90-231)His Prion Protein, cellular formhuman, recombinant, E. coli 5
PR-913 Proteins: native PrPc (globular domain, residues 90-230)His Prion Protein, cellular formmouse, recombinant, E. coli 5
PR-909 Proteins: native PrPc (full length, residues 23-231)His Prion Protein, cellular formhamster, recombinant, E. coli 5
PR-912 Proteins: native PrPc (globular domain, residues 90-231)His Prion Protein, cellular formhamster, recombinant, E. coli 5
PR-910 Proteins: native PrPc (full length, residues 23-230)His Prion Protein, cellular formmouse, recombinant, E. coli 5
PR-908 Proteins: native PrPc (full length, residues 23-231)His Prion Protein, cellular formhuman, recombinant, E. coli 5


 

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