NR ANQR
AU Zeiler,B.; Adler,V.; Kryukov,V.; Grossman,A.
TI Concentration and removal of prion proteins from biological solutions
QU Biotechnology and Applied Biochemistry 2003 Apr; 37(2): 173-82
PT journal article
AB The pathogenesis of prion diseases is characterized by the accumulation of amyloid-like rods or scrapie-associated fibrils. The major protein component of scrapie-associated fibrils is an abnormally folded isoform of the normal cellular prion protein (PrPc) that is resistant to digestion by proteinase K and is referred to as PrPsc. Purified human recombinant ( hr PrP) was used to characterize the binding of a set of RNAs with affinity to PrP proteins. We report here that hr PrP has two RNA-binding activities at physiological pH. One activity is capable of binding all of the screened RNAs with high affinity, whereas the other activity can bind only to a subset of the RNAs with high affinity in the presence of non-specific competitor RNAs. A novel RNA belonging to the latter class, RQ11+12, bound to hr PrP with high affinity in the presence of vast molar excesses of competing RNAs. Beads impregnated with the RQ11+12 RNA were used to construct a filtration column. The column efficiently bound hr PrP and native PrPc from serum and urine. Importantly, the filtration device was also capable of binding proteinase K-treated PrPsc from serum and urine. The level of sensitivity of detection of PrP by standard Western blotting was increased at least 1000-fold by first concentrating PrP from solution with the filtration column.
AD Q-RNA, Inc., 3960 Broadway, New York, NY 10032-1543, U.S.A.
SP englisch
PO England