Enzymatic activity of a subtilisin homolog Tk-SP from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein

摘要

BackgroundTk-SP is a member of subtilisin-like serine proteases from a hyperthermophilic archaeon Thermococcus kodakarensis. It has been known that the hyper-stable protease, Tk-SP, could exhibit enzymatic activity even at high temperature and in the presence of chemical denaturants. In this work, the enzymatic activity of Tk-SP was measured in the presence of detergents and EDTA. In addition, we focused to demonstrate that Tk-SP could degrade the abnormal prion protein (PrP^Sc), a protease-resistant isoform of normal prion protein (PrP^C).