Abstract
Heterogeneity in transmissible spongiform encephalopathy is thought to have derived from conformational variation in an abnormal isoform of the prion protein (PrP Sc). To characterize PrP Sc in bovine spongiform encephalopathy (BSE) and scrapie, we analyzed the newly generated N-terminus of PrP Sc isoforms by digestion with proteinase K (PK). With a lower concentration of PK, the terminal amino acid of BSE PrP Sc converged at N 96. Under the same conditions, however, the terminal amino acid of scrapie PrP Sc was G 81 or G 85. Furthermore, with an increase of PK concentration, the N-terminal amino acid was shifted and converged at G 89. The results suggest that the PK cleavage site of BSE PrP Sc is uniform and is different from the cleavage site of scrapie PrP Sc.
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