Construction of expressing plasmids of recombinant FN polypeptides with bifunctional-domain and the characterization of the products expressed inE. coli
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Two expressing plasmids have been constructed and used to express two bifurictional-domain recombinant polypeptides of human fibronectin (FN) inE. coli. One was CH50 (Pro1239-Ser1515 of FN linked with Ala1690-Thr1960 of FN through Met) and the other was CH56 (Pro1239-Thr1960 of FN). Both of two polypeptides were capable of binding heparin and were purified by heparin-agarose affinity chromatography. The purified products were capable of binding cells. The production of CH50 and CH56 polypeptides provided a fundamental basis for further study of the anti-metastatic function of recombinant fibronectin polypeptides.
Key wordsfibronectin recombinant polypeptide metastasis
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