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Production of biologically active thymulin in Escherichia coli through expression of a chemically synthesized gene

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Summary

A synthetic gene coding for thymulin was ligated into an expression vector (pJB 1301) and placed under lac operon control. In the recombinant clones, thymulin was expressed as part of a β galactosidase chimeric protein which was then cleaved by cyanogen bromide. Thymulin was purified using various chromatography systems including gel filtration and HPLC, and was detected by radioimmunoassay (RIA). In the biological assay the purified recombinant peptide demonstrated the same zinc dependency as natural thymulin and had the same amino acid composition and primary structure.

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Authors and Affiliations

  1. INSERM U 25 et CNRS UA 122 Hopital Necker, 161 rue de Sèvres, 75743, Paris, France

    Alphonse Calenda, Agnès Cordonnier, Florence Lederer, Diep K. H. Le & Jean Marie Pleau

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  1. Alphonse Calenda
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  2. Agnès Cordonnier
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  3. Florence Lederer
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  4. Diep K. H. Le
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  5. Jean Marie Pleau
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Calenda, A., Cordonnier, A., Lederer, F. et al. Production of biologically active thymulin in Escherichia coli through expression of a chemically synthesized gene. Biotechnol Lett 10, 155–160 (1988). https://doi.org/10.1007/BF01134818

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