CHARACTERIZATION OF INVIVO SALIVARY-DERIVED ENAMEL PELLICLE
CHARACTERIZATION OF INVIVO SALIVARY-DERIVED ENAMEL PELLICLE
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DOI：
10.1016/0003-9969(89)90070-8
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发表时间：
1989-01-01
影响因子：
3
通讯作者：
LEVINE, MJ
中科院分区：
文献类型：
--
作者：
ALHASHIMI, I;LEVINE, MJ
唾液蛋白和糖蛋白，参与2小时在体内牙釉质膜的形成，确定利用聚丙烯酰胺凝胶电泳[十二烷基硫酸钠（SDS）-PAGE和阴离子PAGE]/Western转移分析，和特定的放射性标记/SDS-PAGE荧光。这些方法的灵敏度允许识别不同唾液蛋白家族的个体成员。这种薄膜的主要成分是唾液α-淀粉酶、含半胱氨酸的磷蛋白（CCP或胱抑素）、唾液粘蛋白和sIgA。糖基化淀粉酶的存在量大于非糖基化种类。仅鉴定了含半胱氨酸磷蛋白家族的CCPI（半胱氨酸蛋白酶抑制剂SA-I）。检测到较高分子量的唾液粘蛋白（MG 1），但未检测到较低分子量的物质（MG 2）。这些结果扩展了早期的观察唾液蛋白吸附到釉质表面的选择性，证明只有特定的成员唾液蛋白家族参与2小时在体内牙釉质薄膜的形成。研究结果还表明，个别家庭成员可能在口腔中具有不同的功能。
Salivary proteins and glycoproteins that participate in the formation of 2-h in vivo enamel pellicle were determined utilizing polyacrylamide gel electrophoresis [sodium dodecyl sulphate (SDS)-PAGE and anionic PAGE]/Western transfer analyses, and specific radiolabelling/SDS-PAGE fluorography. The sensitivity of these methods permitted the identification of individual members of different salivary protein families. The major components of this pellicle were salivary .alpha.-amylase, cysteine-containing phosphoprotein (CCP or cystatins), salivary mucin and sIgA. Glycosylated amylase was present in larger quantity than the non-glycosylated species. Only CCPI (cystatin SA-I) of the cysteine-containing phosphoprotein family was identified. The higher molecular-weight salivary mucin (MG1), but not the lower molecular-weight species (MG2), was detected. These results extend earlier observations regarding the selective nature of salivary protein adsorption to enamel surface by demonstrating that only specific members of salivary protein families are involved in 2-h in vivo enamel pellicle formation. The findings also suggest that individual family members may have different functions in the mouth.