NR AKSZ
AU Shaked,Y.; Rosenmann,H.; Hijazi,N.; Halimi,M.; Gabizon,R.
TI Copper binding to the PrP isoforms: a putative marker of their conformation and function.
QU Journal of Virology 2001 Sep; 75(17): 7872-4
PT journal article
AB We show here that PrPc, the normal isoform of the prion protein (PrPsc), could be retained by a Cu(2+)-loaded resin through two different binding sites. Contrarily, PrPsc was not retained at all by such resin. This constitutes a new prion-specific property of PrPsc, which in addition to protease resistance and beta-sheet content, may result from its aberrant conformation.
MH Animal; Chromatography, Affinity/methods; Copper/*metabolism; Hamsters; PrPc Proteins/*chemistry/*metabolism; PrPsc Proteins/*chemistry/*metabolism; Protein Conformation; Protein Isoforms/metabolism
AD Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem, Israel.
SP englisch
PO USA