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Fragment of an endogenous inhibitor produced in Escherichia coli for calcium‐activated neutral protease (CANP) retains an inhibitory activity
Author(s) -
Imajoh Shinobu,
Kawasaki Hiroshi,
Emori Yasufumi,
Ishiura Shoichi,
Minami Yasufumi,
Sugita Hideo,
Imahori Kazutomo,
Suzuki Koichi
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80161-8
Subject(s) - escherichia coli , endogeny , protease , biochemistry , inhibitory postsynaptic potential , enzyme , protease inhibitor (pharmacology) , chemistry , microbiology and biotechnology , biology , gene , neuroscience , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology
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.