A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity.
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 structures, inhibits 4 mol CANP. This supports the hypothesis that the repeating unit is the functional unit of inhibition. The results also indicate that post-translational modification of the inhibitor is not essential for inhibition.
D000595:Amino Acid Sequence; D000818:Animals; D002154:Calpain / Q000037:antagonists & inhibitors*; D003001:Cloning, Molecular; D004247:DNA; D004926:Escherichia coli / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology; D010446:Peptide Fragments / Q000096:biosynthesis*; D011817:Rabbits; D013329:Structure-Activity Relationship
D006023:Glycoproteins; D010446:Peptide Fragments; C039304:calpain inhibitors; D004247:DNA; D002154:Calpain