| Autor: |
Takashi Yokoyama, Shirou Mohri, Morikazu Imamura, Yoshifumi Iwamaru, Kentaro Masujin, Kazuo Kasai |
| Jazyk: |
angličtina |
| Rok vydání: |
2013 |
| Předmět: |
|
| Zdroj: |
Pathogens, Vol 2, Iss 1, Pp 92-104 (2013) |
| Druh dokumentu: |
article |
| ISSN: |
2076-0817 |
| DOI: |
10.3390/pathogens2010092 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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