Kahane I, Tully J G
J Bacteriol. 1976 Oct;128(1):1-7. doi: 10.1128/jb.128.1.1-7.1976.
The binding of iodinated wheat germ agglutinin, Ricinus communis agglutinin, and concanavalin A to mycoplasma cells and membranes was examined. All mycoplasmas studied specifically bound concanavalin A or R. communis agglutinin and, to a lesser degree, wheat germ agglutinin. The binding of lectins to whole cells was similar to that recorded for membranes, suggesting that significant binding only occurred on the outer surface of the mycoplasma membrane. Proteolysis of the membrane almost always increased the capacity to bind lectins, which indicates that additional carbohydrate groups on the mycoplasma membrane are masked by a protein layer or protein complexes on the membrane. The observation that carbohydrates are apparently exposed on the surface of mycoplasma membranes should stimulate more concentrated study on the isolation and chemical characterization of these substances since it is quite likely that they are responsible for a variety of reactions between mycoplasmas and host cells.
研究了碘化麦胚凝集素、蓖麻凝集素和伴刀豆球蛋白A与支原体细胞及细胞膜的结合情况。所有研究的支原体都能特异性结合伴刀豆球蛋白A或蓖麻凝集素，且对麦胚凝集素的结合程度较低。凝集素与完整细胞的结合情况与细胞膜的记录相似，这表明显著的结合仅发生在支原体膜的外表面。对细胞膜进行蛋白酶解几乎总能增加其结合凝集素的能力，这表明支原体膜上额外的碳水化合物基团被膜上的蛋白质层或蛋白质复合物所掩盖。碳水化合物显然暴露在支原体膜表面这一观察结果，应该会促使人们更集中地研究这些物质的分离和化学特性，因为它们很可能是支原体与宿主细胞之间各种反应的原因。
