Käsermann F Kempf C 2003 Sodium hydroxide (NaOH) solutions are widely used for the purification of contaminated equipment, as they are known to inactivate a variety of pathogens. However, information about their effect on agents causing transmissible spongiform encephalopathy (TSE) is sparse and contradictory. Scrapie hamster brain homogenate, containing the disease-associated form of the prion protein (PrP(Sc)), was exposed to NaOH. Kinetics studies showed that treatment of brain homogenate with millimolar concentrations of NaOH rapidly abolished the proteinase K-resistant form of the prion protein (PrP(res)). NaOH treatment converted PrP(Sc) into a protease-sensitive form, either in solution or when adsorbed to a metallic surface. If infectivity of TSEs is linked with PrP(res), the results imply that inactivation of TSE occurs more efficiently than currently assumed. https://sonar.ch/global/documents/133018 eng info:eu-repo/semantics/altIdentifier/doi/10.1099/vir.0.19355-0 info:eu-repo/semantics/altIdentifier/pmid/14573823 The Journal of general virology. - 2003 Animals Cricetinae Decontamination Endopeptidase K PrPSc Proteins Sodium Hydroxide Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K. http://purl.org/coar/resource_type/c_6501