Russell M W, Mansson-Rahemtulla B
Oral Microbiol Immunol. 1989 Jun;4(2):106-11. doi: 10.1111/j.1399-302x.1989.tb00107.x.
The potential involvement of surface antigens (Ags) I/II and III of Streptococcus mutans in its adherence to salivary pellicle-coated tooth surfaces was investigated. The binding of radiolabelled Ag I/II to hydroxyapatite was increased by pretreating the mineral with human parotid saliva, and binding was maintained in the continuous presence of saliva. Binding of Ag III to hydroxyapatite was inhibited by pretreatment with, or in the presence of, saliva. Various aminohexoses, and also tris, inhibited the binding of Ag I/II. When Ags I/II and III were tested for their ability to bind to salivary components separated by SDS gel electrophoresis, several proteins capable of binding Ag I/II were identified, notably 2 proteins of apparent relative molecular mass 28,000 and 38,000. Analysis of these proteins, isolated by micro-preparative electrophoresis, indicated high proportions of proline, glycine, and glutamic acid, and overall compositions similar to basic proline-rich salivary proteins.
研究了变形链球菌表面抗原I/II和III在其黏附于唾液薄膜包被的牙齿表面过程中的潜在作用。用人类腮腺唾液预处理矿物质后，放射性标记的抗原I/II与羟基磷灰石的结合增加，且在唾液持续存在的情况下结合得以维持。唾液预处理或在唾液存在时会抑制抗原III与羟基磷灰石的结合。各种氨基己糖以及三羟甲基氨基甲烷会抑制抗原I/II的结合。当检测抗原I/II和III与通过SDS凝胶电泳分离的唾液成分的结合能力时，鉴定出了几种能够结合抗原I/II的蛋白质，特别是两种表观相对分子质量分别为28,000和38,000的蛋白质。对通过微量制备电泳分离得到的这些蛋白质进行分析，结果表明其脯氨酸、甘氨酸和谷氨酸比例较高，总体组成与富含碱性脯氨酸的唾液蛋白相似。
