Expression of Biologically Active Human Calpastatin in Baculovirus-infected Insect Cells and in Escherichia coli

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概要

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• Calpastatin, an endogeneous inhibitor protein acting on calpain (Ca^<2+>-dependent cysteine proteinase), is widely distributed in animal tissues and cells. Two different expression systems, baculovirus-infected Spodoptera frugiperda (Sf9) insect cells and Escherichia coli, were used for overexpression of the human calpastatin tagged with N-terminal hexahistidine peptide. Recombinant calpastatin was purified to homogeneity by nickel ion affinity chromatography and gel filtration separation. Purified recombinant proteins from both systems have similar inhibitory activity for calpain.

• 社団法人日本農芸化学会の論文
• 1998-01-23

著者

• Yokoyama Akiko

  School Of Agricultural Sciences Nagoya University

• Maki M

  Nagoya Univ. Nagoya Jpn

• Maki Masatoshi

  School Of Agricultural Sciences Nagoya University

• Hitomi Kiyotaka

  School Of Agricultural Sciences Nagoya University

関連論文

• Characterization of Human Recombinant Transglutaminase 1 Purified from Baculovirus-infected Insect Cells
• GTP, an Inhibitor of Transglutaminases, is Hydrolyzed by Tissue-type Transglutaminase (TGase 2) but not by Epidermal-type Transglutaminase (TGase 3)
• Characterization og Recombinant Mouse Epidermao-Type Transglutaminase (TGase3) : Regulation of Its Activity by Proteolysis and Guanine Nucleotides
• Caspases Cleave the Amino-Terminal Calpain Inhibitory Unit of Calpastatin during Apoptosis in Human Jurkat T Cells^1
• Expression of Biologically Active Human Calpastatin in Baculovirus-infected Insect Cells and in Escherichia coli

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