NR AMIX
AU Welker,E.; Raymond,L.D.; Scheraga,H.A.; Caughey,B.W.
TI Intramolecular versus intermolecular disulfide bonds in prion proteins
QU The Journal of Biological Chemistry 2002 Sep 6; 277(36): 33477-81
PT journal article
AB Prion protein (PrP) is the major component of the partially protease-resistant aggregate that accumulates in mammals with transmissible spongiform encephalopathies. The two cysteines of the scrapie form, PrPsc, were found to be in their oxidized (i.e. disulfide) form (Turk, E., Teplow, D. B., Hood, L. E., and Prusiner, S. B. (1988) Eur. J. Biochem. 176, 21-30); however, uncertainty remains as to whether the disulfide bonds are intra- or intermolecular. It is demonstrated here that the monomers of PrPsc are not linked by intermolecular disulfide bonds. Furthermore, evidence is provided that PrPsc can induce the conversion of the oxidized, disulfide-intact form of the monomeric cellular prion protein to its protease-resistant form without the temporary breakage and subsequent re-formation of the disulfide bonds in cell-free reactions.
MH Animal; Cell-Free System; Cysteine/*chemistry; Disulfides/metabolism; Electrophoresis, Polyacrylamide Gel; Guanidine/metabolism; Hamsters; Hydrogen-Ion Concentration; Immunoblotting; Oxygen/metabolism; Prions/*chemistry/*metabolism; Protein Binding; Protein Conformation; Sulfhydryl Compounds/metabolism; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA
SP englisch
PO USA