Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain
Copyright policy )Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain
The pathological prion protein, PrPSc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrPSc aggregates of mouse-adapted prion strains. We showed that small PrPSc aggregates, previously thought to be PK-sensitive, are resistant to PK digestion. Furthermore, we showed that small PrPSc aggregates of the Chandler scrapie strain have greater resistance to PK digestion and aggregation-denaturation than large PrPSc aggregates of this strain. We conclude that this strain consists of heterogeneous PrPSc.
prion, conformational stability, small PrP<sup>Sc</sup> aggregate, R, Medicine, Chandler, Article, small PrPSc aggregate, PK sensitivity
prion, conformational stability, small PrP<sup>Sc</sup> aggregate, R, Medicine, Chandler, Article, small PrPSc aggregate, PK sensitivity
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