| Literature DB >> 11483731 |
Y Shaked1, H Rosenmann, N Hijazi, M Halimi, R Gabizon.
Abstract
We show here that PrP(C), the normal isoform of the prion protein (PrP(Sc)), could be retained by a Cu(2+)-loaded resin through two different binding sites. Contrarily, PrP(Sc) was not retained at all by such resin. This constitutes a new prion-specific property of PrP(Sc), which in addition to protease resistance and beta-sheet content, may result from its aberrant conformation.Entities:
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Year: 2001 PMID: 11483731 PMCID: PMC115030 DOI: 10.1128/jvi.75.17.7872-7874.2001
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103