SCRAPIE INFECTIVITY CORRELATES WITH CONVERTING ACTIVITY, PROTEASE RESISTANCE, AND AGGREGATION OF SCRAPIE-ASSOCIATED PRION PROTEIN IN GUANIDINE DENATURATION STUDIES
B. Caughey et al., SCRAPIE INFECTIVITY CORRELATES WITH CONVERTING ACTIVITY, PROTEASE RESISTANCE, AND AGGREGATION OF SCRAPIE-ASSOCIATED PRION PROTEIN IN GUANIDINE DENATURATION STUDIES, Journal of virology, 71(5), 1997, pp. 4107-4110
Denaturation studies with guanidine HCl (GdnHCl) were performed to tes
t the relationship between scrapie infectivity and properties of scrap
ie-associated prion protein (PrPSc). Large GdnHCl-induced reductions i
n infectivity were associated,vith the irreversible elimination of bot
h the proteinase K resistance and apparent self-propagating converting
activity of PrPSc. In intermediate GdnHCl concentrations that stimula
te converting activity and partially disaggregate PrPSc, both scrapie
infectivity and converting activity were associated with residual part
ially protease-resistant multimers of PrPSc.