Purification and properties of serine protease from Halobacterium halobium.

@article{Izotova1983PurificationAP,
  title={Purification and properties of serine protease from Halobacterium halobium.},
  author={Lara S. Izotova and Alexander Ya. Strongin and L N Chekulaeva and V. E. Sterkin and V I Ostoslavskaya and L A Lyublinskaya and E. A. Timokhina and V. M. Stepanov},
  journal={Journal of bacteriology},
  year={1983},
  volume={155 2},
  pages={826-30}
}
Pure extracellular serine protease was isolated from the culture filtrate of Halobacterium halobium by bacitracin-Sepharose affinity chromatography. The enzyme activity was completely and irreversibly lost if the NaCl concentration fell below 2 M. The protease consists of one polypeptide chain with a molecular weight of 41,000. It is characteristically enriched in Asx and Glx content, whereas the level of basic amino acids in the enzyme molecule is unusually low. The protease shows a preference… CONTINUE READING