作者: David L. Linemeyer , Linda J. Kelly , John G. Menke , Guillermo Gimenez-Gallego , Jerry DiSalvo
DOI: 10.1038/NBT0987-960
关键词: FGF10 、 Escherichia coli 、 Gene expression 、 Fibroblast growth factor 、 Biology 、 Molecular biology 、 Fibroblast growth factor receptor 4 、 Expression vector 、 Fibroblast growth factor receptor 3 、 3T3 cells 、 Biochemistry 、 Biotechnology 、 Molecular medicine 、 Applied Microbiology and Biotechnology 、 Bioengineering 、 Biomedical engineering
摘要: A gene encoding bovine acidic fibroblast growth factor has been chemically synthesized, cloned and expressed as a biologically active protein in Escherichia coli. The 440 base pair was assembled by enzymatic ligation of 16 oligonucleotides into pBR322–derived expression plasmid downstream the hybrid tac promoter. Expressed recombinant mitogen comigrated with native brain–derived detected Western blot immunological analysis. product synthetic purified to apparent homogeneity demonstrates mitogenic activity for Balb/c 3T3 cells presence heparin equivalent mitogen. These results demonstrate feasibility expressing large amounts functional bacteria provide system site–specific mutagenesis protein.