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  • Title: High level synthesis of biologically active recombinant trichosanthin in Escherichia coli.
    Author: Zhu RH, Ng TB, Yeung HW, Shaw PC.
    Journal: Int J Pept Protein Res; 1992 Jan; 39(1):77-81. PubMed ID: 1634332.
    Abstract:
    Two forms of recombinant trichosanthin (rTCS) were synthesized in high levels in Escherichia coli by putting the TCS cDNA under the control of a T7 RNA polymerase-directed promoter. Purification schemes were developed to isolate the recombinant protein from both soluble and insoluble fractions. Form I rTCS possessed the mature TCS sequence and had similar biological activities as the natural protein. Its IC50 was approximately 0.13 nM in an in vitro rabbit reticulocyte translational system and a dose of around 35 micrograms protein per 25 g body weight was sufficient to induce complete abortion in mice. Form II rTCS had a propeptide of 19 aa at the C-terminus and was five times less active than Form I in inhibiting protein synthesis by a rabbit reticulocyte lysate.
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