Analysis of Major Surface Polypeptides of Rickettsia japonica

Takahiro Uchida, David H. Walker, Tsuneo Uchiyama

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Major surface polypeptides of Rickettsia japonica migrated to the position of 120,135, and 145 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, when the organisms were solubilized at room temperature. Two major bands at the position of 135 and 185 kDa were seen, when the organisms were solubilized by heating before electrophoresis. Heat-denaturation of the 120-and 145-kDa polypeptides in excised gel bands changed their mobility and caused them to migrate to 135-and 185-kDa positions, respectively. Two polypeptides at the 120-kDa position were demonstrated: one is a major heat-modifiable polypeptide and the other a minor heat-stable. Peptide mapping was performed to determine the identity between native and denatured polypeptides.

Original languageEnglish (US)
Pages (from-to)575-579
Number of pages5
Issue number7
StatePublished - 1994


  • Peptide mapping
  • Rickettsia japonica
  • Spotted fever group rickettsiae
  • Surface polypeptides

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology


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