[Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp. R6-5].

@article{Shi2007PurificationAC,
  title={[Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp. R6-5].},
  author={Wan-liang Shi and Chuan-qi Zhong and Bing Feng Tang and Ping Shen},
  journal={Wei sheng wu xue bao = Acta microbiologica Sinica},
  year={2007},
  volume={47 1},
  pages={161-3}
}
A halophilic extracellular protease from a halophilic archaea Natrinema sp. R6-5 was purified to SDS-PAGE homogeneity using bacitracin-Sepharose 4B chromatography. A molecular mass of the purified protease subunit was 62KD determined by SDS-PAGE. The protease activity was inhibited by phenylmethylsulfonyl fluoride (PMSF), suggesting that the protease belong to serine protease. The protease exhibited optimum NaCl concentration is 3 mol/L. At the 3 mol/L NaCl concentration, the optimum… CONTINUE READING