Sawa Y, Watanabe T, Shibata K
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Japan.
Microbiol Immunol. 1992;36(6):655-9. doi: 10.1111/j.1348-0421.1992.tb02067.x.
Cell proteins of Mycoplasma salivarium were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to membranes, then examined for reactivity with human IgG molecules, the Fc fragment of human IgG, and concanavalin A (ConA). Multiple protein bands bound IgG, and most of them also bound ConA. One (corresponding to a molecular mass of 90 kDa) of the IgG- and ConA-binding bands intensely interacted with the Fc fragment of IgG. The reactivity of proteins eluted from the band with the Fc fragment, tested by dot-blotting and ELISA, was inhibited (90%) by pre-incubation with IgG and to a lesser extent (50%), with IgM. Thus, M. salivarium contained a cellular protein with a molecular mass of 90 kDa, that bound the Fc fragment of human IgG.
唾液支原体的细胞蛋白通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行分离，转移至膜上，然后检测其与人IgG分子、人IgG的Fc片段以及伴刀豆球蛋白A（ConA）的反应性。多条蛋白带与IgG结合，并且它们中的大多数也与ConA结合。其中一条IgG和ConA结合带（对应分子量为90 kDa）与IgG的Fc片段强烈相互作用。通过斑点印迹法和酶联免疫吸附测定法检测，从该条带洗脱的蛋白与Fc片段的反应性在与IgG预孵育后受到抑制（90%），而与IgM预孵育时抑制程度较小（50%）。因此，唾液支原体含有一种分子量为90 kDa的细胞蛋白，该蛋白与人IgG的Fc片段结合。
