Abstract.
An efficient Escherichia coli expression system for the production of a perchloric acid-soluble protein (PSP) has been constructed. Complementary DNA encoding PSP was inserted into an inducible bacterial expression vector pGEX-4T-1. After the plasmid introduced into E. coli was expressed by isopropyl 1-thio-β-D-galactopyranoside (IPTG), the recombinant product was purified by glutathione-Sepharose 4B affinity chromatography. The purified product showed the expected NH2-terminal sequence, but the translation inhibitory activity of this product was 10 times lower compared with that of authentic PSP isolated from rat liver.
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Received 8 October 1998; received after revision 6 November 1998; accepted 6 November 1998
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Oka, T., Nishimoto, Y., Sasagawa, T. et al. Production of functional rat liver PSP protein in Escherichia coli. CMLS, Cell. Mol. Life Sci. 55, 131–134 (1999). https://doi.org/10.1007/s000180050277
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DOI: https://doi.org/10.1007/s000180050277