Russell R R, Donald A C, Douglas C W
J Gen Microbiol. 1983 Oct;129(10):3243-50. doi: 10.1099/00221287-129-10-3243.
Streptococcus mutans serotype c produces several extracellular proteins which bind to affinity columns of immobilized glucans. The proteins are three distinct glucosyltransferases and another glucan-binding protein (molecular weight 74000) which is now shown to be a fructosyltransferase. This enzyme is antigenically distinct and genetically independent of two other fructosyltransferases produced by the same organism. A mutant is described which lacks the glucan binding fructosyltransferase and has defective ability to form adherent colonies in the presence of sucrose. Although the production of glucans from sucrose results in the glucan binding protein becoming bound to the bacterial surface, and hence perhaps contributing to adherence, the fructans synthesized by the enzyme do not appear to contribute to this phenomenon.
变形链球菌c血清型产生几种细胞外蛋白，这些蛋白可与固定化葡聚糖的亲和柱结合。这些蛋白是三种不同的葡糖基转移酶和另一种葡聚糖结合蛋白（分子量74000），现已证明它是一种果糖基转移酶。该酶在抗原性上与同一生物体产生的另外两种果糖基转移酶不同，并且在遗传上独立。描述了一种突变体，它缺乏葡聚糖结合果糖基转移酶，并且在蔗糖存在下形成粘附菌落的能力有缺陷。虽然由蔗糖产生葡聚糖导致葡聚糖结合蛋白与细菌表面结合，因此可能有助于粘附，但该酶合成的果聚糖似乎对这种现象没有贡献。
