Construction of expressing plasmids of recombinant FN polypeptides with bifunctional-domain and the characterization of the products expressed in E. coli.
Two expressing plasmids have been constructed and used to express two bifunctional-domain recombinant polypeptides of human fibronectin (FN) in E. 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.
Feng
Z
Z
Department of Medical Molecular Biology, Tongji Medical University, Wuhan.
Zhang
G
G
Li
D
D
Zhang
H
H
D004926:Escherichia coli / Q000235:genetics; D005353:Fibronectins / Q000096:biosynthesis*; D006801:Humans; D010446:Peptide Fragments / Q000096:biosynthesis / Q000235:genetics; D010957:Plasmids / Q000235:genetics; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis; D014162:Transfection; D018909:src Homology Domains
D005353:Fibronectins; D010446:Peptide Fragments; D011994:Recombinant Proteins