Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790.

@article{Yamamoto1993PurificationAS,
  title={Purification and specificity of a cell-wall-associated proteinase from Lactobacillus helveticus CP790.},
  author={Naoyuki Yamamoto and A Akino and Toshiaki Takano},
  journal={Journal of biochemistry},
  year={1993},
  volume={114 5},
  pages={740-5}
}
A cell-wall-associated proteinase from Lactobacillus helveticus CP790, grown in skim milk, was purified to homogeneity by DEAE ion exchange chromatography in the presence of EDTA. Its molecular weight was estimated to be 45,000 by SDS-PAGE and also by the recovery of proteinase activity only from this fraction of SDS-PAGE gel slices of crude extract. It had maximum activity at pH 6.5 and 42 degrees C. Since the activity was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), it was… CONTINUE READING