Purification and Characterization of Membrane Protein (90kDa) from <i>Mycoplasma salivarium</i>, Which Binds Immunoglobulin (Ig) G Fc Fragment

J-STAGE
  • Sawa Yoshihiko
    Department of Oral Bacteriology, Hokkaido University School of Dentistry
  • Shibata Ken-ichiro
    Department of Oral Bacteriology, Hokkaido University School of Dentistry
  • Noda Mamoru
    Department of Operative Dentistry, Hokkaido University School of Dentistry
  • Watanabe Tsuguo
    Department of Oral Bacteriology, Hokkaido University School of Dentistry

抄録

A 90kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.

収録刊行物

詳細情報 詳細情報について

問題の指摘

ページトップへ