Purification and characterization of a cell wall proteinase fromStreptococcus lactisNCDO 763

Abstract
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·–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 ∼ 80000.

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