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

被引：108

作者：

Caughey, B ^{[1
]}

Raymond, GJ ^{[1
]}

Kocisko, DA ^{[1
]}

Lansbury, PT ^{[1
]}

机构：

[1] MIT,DEPT CHEM,CAMBRIDGE,MA 02139

来源：

JOURNAL OF VIROLOGY | 1997年 / 71卷 / 05期

关键词：

D O I：

10.1128/JVI.71.5.4107-4110.1997

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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

引用

页码：4107 / 4110

页数：4

共 25 条

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