Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 11 December 1981:
Vol. 214. no. 4526, pp. 1259 - 1261
DOI: 10.1126/science.6795721
Prev | Table of Contents | Next

Articles

Science, Vol 214, Issue 4526, 1259-1261
Copyright © 1981 by American Association for the Advancement of Science

articles

Reversible chemical modification of the scrapie agent

MP McKinley, FR Masiarz, and SB Prusiner

The scrapie agent causes a degenerative nervous system disease in sheep and goats. Studies with extensively purified preparations demonstrated that the agent contains a protein that is required for infectivity. Chemical modification of the scrapie agent by diethyl pyrocarbonate reduced the titer 1000-fold. Exposure of the inactivated agent to hydroxylamine, a strong nucleophile, resulted in complete restoration of infectivity. Presumably, nucleophilic residues within a scrapie agent protein undergo carbethoxylation on reaction with diethyl pyrocarbonate, and subsequent addition of hydroxylamine displaces these carbethoxy groups.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Inactivation of Prions by Acidic Sodium Dodecyl Sulfate.
D. Peretz, S. Supattapone, K. Giles, J. Vergara, Y. Freyman, P. Lessard, J. G. Safar, D. V. Glidden, C. McCulloch, H.-O. B. Nguyen, et al. (2006)
J. Virol. 80, 322-331
   Abstract »    Full Text »    PDF »
Characterization of Thermodynamic Diversity between Transmissible Spongiform Encephalopathy Agent Strains and Its Theoretical Implications.
R. A. Somerville, R. C. Oberthur, U. Havekost, F. MacDonald, D. M. Taylor, and A. G. Dickinson (2002)
J. Biol. Chem. 277, 11084-11089
   Abstract »    Full Text »    PDF »
Identification of a protein that purifies with the scrapie prion.
D. Bolton, M. McKinley, and S. Prusiner (1982)
Science 218, 1309-1311
   Abstract »    PDF »
Novel proteinaceous infectious particles cause scrapie.
S. Prusiner (1982)
Science 216, 136-144
   Abstract »    PDF »
Mapping Cu(II) Binding Sites in Prion Proteins by Diethyl Pyrocarbonate Modification and Matrix-assisted Laser Desorption Ionization-Time of Flight (MALDI-TOF) Mass Spectrometric Footprinting.
K. Qin, Y. Yang, P. Mastrangelo, and D. Westaway (2002)
J. Biol. Chem. 277, 1981-1990
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)