Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCC 14580.

@article{Kakudo1992PurificationCC,
  title={Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCC 14580.},
  author={Shinji Kakudo and Norihiro Kikuchi and Kengo Kitadokoro and Toshimichi Fujiwara and Eiichi Nakamura and Hironori Okamoto and Masateru Shin and Masakatsu Tamaki and Hirobumi Teraoka and Hiroshige Tsuzuki},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 33},
  pages={23782-8}
}
A glutamic acid-specific protease has been purified to homogeneity from Bacillus licheniformis ATCC 14580 utilizing Phe-Leu-D-Glu-OMe-Sepharose affinity chromatography and crystallized. The molecular weight of the protease was estimated to be approximately 25,000 by SDS-polyacrylamide gel electrophoresis. This protease, which we propose to call BLase (glutamic acid-specific protease from B. licheniformis ATCC 14580), was characterized enzymatically. Using human parathyroid hormone (13-34) and p… CONTINUE READING

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