NR AQLM
AU Kim,C.; Morre,D.J.
TI Prion proteins and ECTO-NOX proteins exhibit similar oscillating redox activities
QU Biochemical and Biophysical Research Communications 2004 Mar 19; 315(4): 1140-6
PT journal article
AB Both recombinant full-length mouse prion protein expressed in Escherichia coli and native prion protein (PrPsc) from mouse brain exhibited NADH oxidase and protein disulfide-thiol interchange activities similar to those formerly thought to be properties exclusive to the growth-related, cell surface ECTO-NOX proteins. The two activities exhibited the complex 2+3 pattern of oscillations characteristic of ECTO-NOX proteins where the two activities alternate to generate a period length of 24 min. The oscillations were augmented by copper and diminished by addition of the copper chelator bathocuproene. That the activity might be attributable to a contaminating protein was ruled out by experiments where the purified recombinant prion-containing extracts were resolved by SDS-PAGE and the activity was restricted to a single band corresponding to the predicted Mr of the recombinant prion as verified by Western blot analyses.
MH Animals; Cell Membrane/*metabolism; Chelating Agents/pharmacology; Chromatography, Liquid/methods; Copper/metabolism; Escherichia coli/metabolism; Mice; NADH, NADPH Oxidoreductases/*metabolism; Oxidation-Reduction; Periodicity; PrPsc Proteins/metabolism; Prions/genetics/*metabolism; Protein Disulfide-Isomerase/metabolism; Recombinant Proteins/genetics/metabolism; Spectrophotometry/methods; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.
AD Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907-2064, USA
SP englisch
PO USA