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Correia, F.F.,Waterbury, T.L.,Rosan, B.,DiRienzo, J.M. Korean Academy of Oral Biology and the UCLA Dental 2001 International Journal of Oral Biology Vol.26 No.1
The major outer membrane porin, FomA, from Fusobacterium mucleatum ATCC 10953 was previously shown to be a coaggregation receptor for Streptococcus crista CC5A. The fomA gene was amplified by PCR and cloned in Escherichia coli. The nucleotide sequence of the recombinant gene contained a three base pair deletion and four single base differences compared to the native fomA sequence. The recombinant gene product was glutathione-S-transferase (GST). The GST portion was removed by treatment with thrombin and the FomA portion purified in milligram quantities. The purified recombinant protein contained a glycylserine dipeptide at its amino terminus, bound IgG from antiserum made against native FomA, and retained the heat-modifiable property of the native protein. However, the recombinant FomA failed to bind to S. crista CC5A or inhibit coaggregation between this bacterium and F. nucleatum. FomA may require outer membrane components, such as lipopolysaccharide, to stabilize the protein in a structure recognized by the streptococcal adhesin.