Open AccessCopper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function
Author(s) -
Yuval Shaked,
Hana Rosenmann,
Nuha Hijazi,
Michele Halimi,
Ruth Gabizon
Publication year - 2001
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.75.17.7872-7874.2001
Subject(s) - gene isoform , biology , protease , plasma protein binding , function (biology) , prion protein , biochemistry , microbiology and biotechnology , enzyme , gene , medicine , disease , pathology
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.