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A C-terminal fragment of an endogenous rabbit liver inhibitor for calcium-activated neutral protease (CANP) was produced in Escherichia coli and its inhibitory activity was examined after purification. The truncated inhibitor (373 amino acid residues), which contains two internal repeat structures, inhibits 2 mol CANP whereas the native liver inhibitor (639 residues), containing four internal repeat...
The active site of calcium-activated neutral protease (CANP) was specifically labeled with iodoacetic acid. The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined. The sequence indicates that CANP is a thiol protease and its comparison with other thiol proteases is described.
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