All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II

FEBS Letters

Takano, Emiko²  Hatanaka, Masakazu¹  Maki, Masatoshi¹  Mori, Hirotaka²  Murachi, Takashi²  Sato, Akihiko¹ 

[1] Institute for Virus Research, Faculty of Medicine, Kyoto University, Kyoto 606 Japan;Department of Clinical Science and Laboratory Medicine, Faculty of Medicine, Kyoto University, Kyoto 606 Japan

关键词: Calpastatin;    cDNA;    Expression;    Proteinase inhibitor;   

DOI  :  10.1016/0014-5793(87)80531-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complementary DNA portions coding for each domain (domain L internally repetitive domains, domains 1–4, each composed of approximately 140 amino acid residues) of pig calpastatin were subcloned into E. coli plasmids to express the respective portions of the proteinase inhibitor gene in bacteria. Cell extracts of E. coli harboring recombinant plasmids were assayed for calpain inhibition. All four internally repetitive domains showed inhibitory activities, essentially similar to one another, against calpains I and II. No inhibition was observed in the case of the N-terminal non-homologous domain (domain L). These results support our previous conclusion that the repetitive region is a functional unit of the proteinase inhibitor.

【 授权许可】

Unknown