Modified penicillin acylase signal peptide allows the periplasmic production of soluble human interferon-γ but not of soluble human interleukin-2 by the Tat pathway in Escherichia coli
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Production of periplasmic human interferon-γ (hINF-γ) and human interleukin-2 (hIL-2) by the Tat translocation pathway in Escherichia coli BL21-SI was evaluated. The expression was obtained using the pEMR vector which contains the Tat-dependent modified penicillin acylase signal peptide (mSPpac) driven by the T7 promoter. The mSPpac-hINF-γ was processed and the protein was transported to periplasm. Up to 30.1%25 of hINF-γ was found in the periplasmic soluble fraction, whereas only 15%25 of the mSPpac-hIL-2 was processed, but hIL-2 was not found in the periplasmic soluble fraction. © 2007 Springer Science%2bBusiness Media B.V.
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Periplasm; Signal peptide; Tat pathway; Therapeutic protein Enzyme activity; Escherichia coli; Gamma rays; Peptides; Polypeptides; Solubility; Periplasm; Signal peptide; Tat pathway; Therapeutic protein; Translocation pathway; Interferons; gamma interferon; interleukin 2; recombinant protein; article; chemistry; cytoplasm; Escherichia coli; genetics; human; metabolism; methodology; physiology; protein engineering; solubility; Escherichia coli; Humans; Interferon Type II; Interleukin-2; Periplasm; Protein Engineering; Recombinant Proteins; Solubility; Escherichia coli
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