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  • Title: [Construction, expression and functional characterization of disulfide-stabilized anti-hepatocarcinoma single chain Fv fused with truncated Pseudomonas exotoxin].
    Author: Zhao J, Sun ZW, Liu YF, Yu WY.
    Journal: Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi; 2003 Nov; 19(6):585-7. PubMed ID: 15182657.
    Abstract:
    AIM: To prepare fusion protein of disulfide-stabilized anti-hepatocarcinoma single chain Fv(dsFv)and truncated Pseudomonas exotoxin(PE38). METHODS: The gene encoding the fusion protein was cloned into the prokaryotic expression vector pTIG which was then transformed into E.coli origami(DE3). The expressed product was purified through Ni-NTA agarose affinity chromatography column. The cytotoxicity of the purified dsFv-PE38 was detected by MTT colorimetry. RESULTS: The immunotoxin dsFv PE38 was expressed in E.coli origami(DE3) in a soluble form, which accounted for nearly 21% of the total bacterial soluble proteins. The results of cytotoxic assay showed that the dsFv-PE38 could specifically kill hepatocarcinoma cells, while spared the normal hepatic cells. CONCLUSION: The immunotoxin dsFv-PE38 may have some potential value in the treatment of hepatocarcinoma.
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