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α-Enolase is an important glycol tic enzyme. It is present in the cytoplasm of prokaryotic as.well as eukaryotic cells and is a protein with many functions. a-Enolase is expressed on several cell surface, where it acts as a plasminogen receptor, hydrolyzing the in active plasminogen in to active proteolysis plasmid. In addition to being used in glycolysis, α-Enolase also performs the function of a plasminogen receptor. It also performs other cellular functions and is present at varying sub cellular localizations. The degree of the difference of expression of α-enolase has been associated to more than a few diseases, like cancer, alzheimer's disease, and rheumatoid arthritis. In this study, α-enolase is identified as a plasminogen receptor in numerous types of cells. Specifically, its function has been recognized in my genesis as an instance of extracellular remodeling procedure.α-Enolase is present on the surface of the cell of differentiating myocytes. Inhibitors of α-enolase plasminogen binding block fusion of myogenic in vitro and regeneration of skeletal muscle in mice.This study uses: genomic DNA as a template to amplify the full-length DNA sequence enolase by PCR to pET28a(+) as the carrier, recombinant plasmid transformed in to E.coli BL21(DE3), and IPTG induction of recombinant fusion protein expression. Western blot identification is performed, and affinity chromatography purification of recombinant proteins with anti- his tag monoclonal antibodies and antibody- positive patients with Candida albicans serum..And in my study it could be determined that 6 hours and 37℃ provided the best expression on α-enolase enzyme time..Key words: α-enolase, protein expression ,gene cloning, enzyme characterization
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