Hitomi K, Yokoyama A, Maki M
School of Agricultural Sciences, Nagoya University, Japan.
Biosci Biotechnol Biochem. 1998 Jan;62(1):136-41. doi: 10.1271/bbb.62.136.
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.
