Purification and characterization of a cell wall proteinase from Streptococcus lactis NCDO 763.

@article{Monnet1987PurificationAC,
  title={Purification and characterization of a cell wall proteinase from Streptococcus lactis NCDO 763.},
  author={V{\'e}ronique Monnet and Daniel Le Bars and J-C. Gripon},
  journal={The Journal of dairy research},
  year={1987},
  volume={54 2},
  pages={247-55}
}
A proteinase was purified from a cell wall extract of a culture of Streptococcus lactis NCDO 763 grown in skim milk. Being active at a low pH (at pH 4.8 on haemoglobin and pH 6.0-6.5 on casein) and completely inhibited by diisopropylfluorophosphate, it was considered to be a serine proteinase partly inhibited by EDTA; the mol. wt was approximately 80,000. 

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