EC Number   |
Application |
Reference |
|---|
   3.4.21.B57 | medicine |
potential application for the inactivation of abnormal prion protein PrPSc, a protease-resistant isoform of normal prion protein. PrPSc is largely unaffected by standard methods of sterilization, thus, contaminated neurosurgical instruments are the major cause of human transmissible spongiform encephalopathies |
727248 |
| 3.4.21.B57 | medicine |
the abnormal prion protein (scrapie-associated prion protein, PrP(Sc)) is considered to be included in the group of infectious agents of transmissible spongiform encephalopathies. Since PrP(Sc) is highly resistant to normal sterilization procedures, the decontamination of PrP(Sc) is a significant public health issue. The hyperthermostable protease, Tk-subtilisin, can be an effective agent for medical decontamination of of PrP(Sc). Rather small amounts of Tk-subtilisin (0.3 U) are required to degrade PrP(Sc) at 100 °C and pH 8.0. In addition, Tk-subtilisin is observed to degrade PrP(Sc) in the presence of sodium dodecyl sulfate or other industrial surfactants. Basic information for the practical use of the proteolytic enzyme for PrP(Sc) degradation is provided |
726790 |
| 3.4.21.B57 | medicine |
the enzyme may have potential application as a detergent additive to decrease the infectivity of abnormal prion protein PrPSc |
727248 |
| 3.4.21.B57 | medicine |
Tk-SP-containing detergents can be developed to decrease the secondary infection risks of transmissible spongiform encephalopathies |
727248 |
