%0 Journal Article
%T Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain
%A Kazuo Kasai
%A Yoshifumi Iwamaru
%A Kentaro Masujin
%A Morikazu Imamura
%A Shirou Mohri
%A Takashi Yokoyama
%J Pathogens
%D 2013
%I MDPI AG
%R 10.3390/pathogens2010092
%X The pathological prion protein, PrP Sc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrP Sc aggregates of mouse-adapted prion strains. We showed that small PrP Sc aggregates, previously thought to be PK-sensitive, are resistant to PK digestion. Furthermore, we showed that small PrP Sc aggregates of the Chandler scrapie strain have greater resistance to PK digestion and aggregation-denaturation than large PrP Sc aggregates of this strain. We conclude that this strain consists of heterogeneous PrP Sc.
%K prion
%K Chandler
%K small PrPSc aggregate
%K conformational stability
%K PK sensitivity
%U http://www.mdpi.com/2076-0817/2/1/92