All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
Year: 1987
Type: article
Abstract: Complementary DNA portions coding for each domain (domain L and 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.
Source: FEBS Letters
Authors: Masatoshi Maki, Emiko Takano, Hirotaka Mori, Akihiko Sato, Takashi Murachi, Masakazu Hatanaka
Institution: Kyoto University
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2072665632