Fragment of an endogenous inhibitor produced in Escherichia coli for calcium‐activated neutral protease (CANP) retains an inhibitory activity

FEBS Letters

Sugita, Hideo³  Kawasaki, Hiroshi¹  Minami, Yasufumi¹  Imahori, Kazutomo²  Ishiura, Shoichi³  Imajoh, Shinobu¹  Emori, Yasufumi¹  Suzuki, Koichi¹ 

[1] Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113, Japan;Mitsubishi-Kasei Institute of Life Sciences, Minamiooya, Machida-shi, Tokyo 194, Japan;National Center of Neurology and Psychiatry, Kodaira, Tokyo 187 Japan

关键词: Ca2+-activated neutral protease;    Calpain;    Proteinase inhibitor;   

DOI  :  10.1016/0014-5793(87)80161-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown