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Literature summary for 3.4.24.27 extracted from

  • Cronier, S.; Gros, N.; Tattum, M.H.; Jackson, G.S.; Clarke, A.R.; Collinge, J.; Wadsworth, J.D.
    Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin (2008), Biochem. J., 416, 297-305.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
analysis thermolysin degrades cellular prion protein while preserving both proteinase K-sensitive and proteinase K-resistant isoforms of disease-related prion protein in both rodent and human prion strains. In variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only about 15% of this material resists digestion by proteinase K Bacillus thermoproteolyticus
medicine thermolysin degrades cellular prion protein while preserving both proteinase K-sensitive and proteinase K-resistant isoforms of disease-related prion protein in both rodent and human prion strains. In variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only about 15% of this material resists digestion by proteinase K Bacillus thermoproteolyticus

Organism

Organism UniProt Comment Textmining
Bacillus thermoproteolyticus P00800
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Bacillus thermoproteolyticus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellular prion protein + H2O thermolysin degrades cellular prion protein while preserving both proteinase K-sensitive and proteinase K-resistant isoforms of disease-related prion protein in both rodent and human prion strains. In variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only about 15% of this material resists digestion by proteinase K Bacillus thermoproteolyticus ?
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