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- W2079555568 abstract "A cytoplasmic protease was partially purified from Escherichia coli; its sedimentation coefficient was found to be 5.3 S. This enzyme (which we call protease A) is not a serine protease and cysteine is not required for its activity; it is only active in the presence of divalent ions which are strongly bound to it. After inactivation of protease A by incubation at 50°C in the presence of 1 mM EDTA, the enzyme is reactived by Mg2+, Mn2+ or Ca2+. We have tried most of the usual esters as substrates and found that none was hydrolyzed by the enzyme which induces a highly restricted specificity." @default.
- W2079555568 created "2016-06-24" @default.
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- W2079555568 date "1975-06-01" @default.
- W2079555568 modified "2023-09-23" @default.
- W2079555568 title "Properties of a Cytoplasmic Proteolytic Enzyme from Escherichia coli" @default.
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- W2079555568 doi "https://doi.org/10.1111/j.1432-1033.1975.tb04155.x" @default.
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