NR AIFJ
AU McKinley,M.P.; Bolton,D.C.; Prusiner,S.B.
TI A protease-resistant protein is a structural component of the scrapie prion
QU Cell 1983 Nov; 35(1): 57-62
PT journal article
AB Fractions purified from scrapie-infected hamster brain contain a unique protein, designated PrP. It was labeled with N-succinimidyl 3-(4-hydroxy-5-[125I]-iodophenyl) propionate, which did not alter the titer of the scrapie prion. The concentration of PrP was found to be directly proportional to the titer of the infectious prion. Both PrP and prion infectivity were resistant for 2 hr at 37 degrees C to hydrolysis by proteinase K under nondenaturing conditions. Prolonging the digestion resulted in a concomitant decrease in both PrP and the scrapie prion. When the amino-acid-specific proteases trypsin or SV-8 protease were used instead of proteinase K, no change in either PrP or the prion was detected. The parallel changes between PrP and the prion provide evidence that PrP is a structural component of the infectious prion. Our findings also suggest that the prion contains only one major protein, namely PrP.
IN Die Infektiosität von Hamster-Prion-Präparationen erwies sich als direkt proportional zur Konzentration des Prionproteins. Das Prionprotein und die Infektiosität erwiesen sich als resistent gegenüber eine zweistündige Inkubation mit Proteinase K bei 37° unter nicht denaturierenden Bedingungen. Bei längeren Verdaus mit Proteinase K, nicht jedoch mit SV-8-Protease nahmen die Menge des Prionproteins und die Infektiosität ab.
MH Endopeptidase K; Endopeptidases/metabolism; Peptide Hydrolases/metabolism; Prions/*analysis; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Trypsin/metabolism; Viral Proteins/*analysis/metabolism; Viral Structural Proteins
SP englisch
PO USA