| First Author | Kim C | Year | 2004 |
| Journal | Biochem Biophys Res Commun | Volume | 315 |
| Issue | 4 | Pages | 1140-6 |
| PubMed ID | 14985132 | Mgi Jnum | J:88593 |
| Mgi Id | MGI:3035848 | Doi | 10.1016/j.bbrc.2004.02.007 |
| Citation | Kim C, et al. (2004) Prion proteins and ECTO-NOX proteins exhibit similar oscillating redox activities. Biochem Biophys Res Commun 315(4):1140-6 |
| abstractText | 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. |
