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. 1997 May;71(5):4107–4110. doi: 10.1128/jvi.71.5.4107-4110.1997

Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.

B Caughey 1, G J Raymond 1, D A Kocisko 1, P T Lansbury Jr 1
PMCID: PMC191566  PMID: 9094691

Abstract

Denaturation studies with guanidine HCl (GdnHCl) were performed to test the relationship between scrapie infectivity and properties of scrapie-associated prion protein (PrP(Sc)). Large GdnHCl-induced reductions in infectivity were associated with the irreversible elimination of both the proteinase K resistance and apparent self-propagating converting activity of PrP(Sc). In intermediate GdnHCl concentrations that stimulate converting activity and partially disaggregate PrP(Sc), both scrapie infectivity and converting activity were associated with residual partially protease-resistant multimers of PrP(Sc).

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Selected References

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