@article{oai:nagasaki-u.repo.nii.ac.jp:00025211,
 author = {Ehara, Masahiko and Ichinose, Yoshio and Iwami, Mamoru and Utsunomiya, Akiyoshi and Shimotori, Shoichi},
 issue = {3},
 journal = {熱帯医学 Tropical medicine},
 month = {Sep},
 note = {A DNA-Binding protein was purified from the cell-surface of Vibrio cholerae O1 by Cellulofine Sulfate affinity chromatography and reversed-phase HPLC. The DNA-binding protein of V. cholerae O1 showed a molecular weight of 9 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Treatment of the protein with cold acetone and 6 M guanidine-HCl produced little change in the DNA-binding activity of the protein. The binding of the protein to supercoiled plasmid DNA as well as to double-stranded short chromosomal DNA fragments has been demonstrated by gel retardation assay and by labeling of the transblotted protein with non-radioactive DNA. N-terminal amino acid sequence of the protein showed a high degree of homology with that of HU 2 (Laine et al., 1978), NS2 (Mende et al., 1978) from Escherichia coli. Indirect immunocytochemical labeling of ultrathin sections of Lowicryl-embedded V. cholerae O1 cells with the antibody against the protein revealed that the protein associates with bulk DNA and also lies at the cell-surface., 熱帯医学 Tropical medicine 33(3). p67-82, 1991},
 pages = {67--82},
 title = {Purification and Characterization of a DNA-Binding Protein of Vibrio cholerae O1},
 volume = {33},
 year = {1991}
}