Sawa Y, Shibata K, Noda M, Watanabe T
Department of Oral Bacteriology, Hokkaido University School of Dentistry, Sapporo, Japan.
Microbiol Immunol. 1994;38(4):257-62. doi: 10.1111/j.1348-0421.1994.tb01773.x.
A 90 kDa 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.
用曲拉通X-100从唾液支原体的细胞膜中释放出一种90 kDa的蛋白质，并通过离子交换色谱法和色谱聚焦法进行纯化。该蛋白质通过色谱聚焦在pH 5.5时被洗脱。结果表明，该蛋白质能与人及9种不同动物物种的IgG的Fc片段发生反应，且不能区分不同物种的IgG，而作为对照测试的蛋白A对人及猪的IgG表现出很强的特异性。此外，该蛋白质还与抗原特异性山羊IgG（对人IgG的γ链具有特异性）、用兔抗绵羊红细胞抗血清致敏的绵羊红细胞（SRBC），即兔IgG的Fc部分以及伴刀豆球蛋白A发生反应。这些发现可能表明该蛋白质是一种凝集素，它能结合IgG Fc部分的碳水化合物部分。
