The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie
| Autor: | Morikazu Shinagawa, Hiroko Hayashi, Yuko Ushiki, Morikazu Imamura, Yoshifumi Iwamaru, Masuhiro Takata, Takashi Yokoyama |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
PrPSc Proteins
Protein Conformation animal diseases Bovine spongiform encephalopathy Molecular Sequence Data Biophysics Scrapie Cleavage (embryo) Biochemistry Protein structure Sequence Analysis Protein medicine Animals Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites Transmissible spongiform encephalopathy Sequence Homology Amino Acid biology Chemistry Cell Biology medicine.disease Proteinase K Virology nervous system diseases Amino acid Encephalopathy Bovine Spongiform nervous system biology.protein Cattle Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 328:1024-1027 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2005.01.065 |
| Popis: | Heterogeneity in transmissible spongiform encephalopathy is thought to have derived from conformational variation in an abnormal isoform of the prion protein (PrPSc). To characterize PrPSc in bovine spongiform encephalopathy (BSE) and scrapie, we analyzed the newly generated N-terminus of PrPSc isoforms by digestion with proteinase K (PK). With a lower concentration of PK, the terminal amino acid of BSE PrPSc converged at N96. Under the same conditions, however, the terminal amino acid of scrapie PrPSc was G81 or G85. Furthermore, with an increase of PK concentration, the N-terminal amino acid was shifted and converged at G89. The results suggest that the PK cleavage site of BSE PrPSc is uniform and is different from the cleavage site of scrapie PrPSc. |
| Databáze: | OpenAIRE |
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