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

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.