Comparison of amylase-binding proteins in oral streptococci.
Comparison of amylase-binding proteins in oral streptococci.
复制标题
口腔链球菌淀粉酶结合蛋白的比较。
DOI：
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发表时间：
1994
影响因子：
2.1
通讯作者：
C. Douglas
中科院分区：
文献类型：
--
作者：
J. Gwynn;C. Douglas
某些种类的口腔链球菌将唾液淀粉酶结合到它们的细胞表面。用配基印迹法比较了一系列链球菌产生的淀粉酶结合蛋白的模式，并研究了结合蛋白的几个特征。戈登链球菌是最均一种，几乎所有菌株都能产生迁移性蛋白质，分子量分别为82 kDa和20 kDa。其他物种的异质性更强，释放的蛋白质在87或82 kDa和/或20至36 kDa之间分解。淀粉酶抑制剂、淀粉酶底物和高碘酸盐处理可阻止淀粉酶与配体印迹上的82/87 kDa蛋白质结合，但对淀粉酶与20-36 kDa蛋白质的结合影响有限或没有影响。Gordonii Challis的20 kDa蛋白在82 kDa蛋白之前被释放到培养基中。这些数据表明，在链球菌中，淀粉酶结合蛋白存在显著差异，高分子和低分子蛋白质与唾液淀粉酶相互作用的方式不同。
Certain species of oral streptococci bind salivary amylase to their cell surface. The patterns of amylase-binding proteins produced by a range of streptococci have been compared by ligand blotting and several characteristics of the binding proteins investigated. Streptococcus gordonii was the most homogeneous species and almost all strains produced proteins migrating with molecular mass 82 kDa and 20 kDa. Other species were more heterogeneous, releasing proteins that resolved at 87 or 82 kDa and/or between 20 and 36 kDa. Binding of amylase to the 82/87-kDa proteins on ligand blots was prevented by amylase inhibitors, amylase substrates and periodate treatment but these had limited or no effect on amylase binding to 20-36 kDa proteins. Also, the 20 kDa protein of S. gordonii Challis was released into culture medium before the 82-kDa protein. These data suggest that there is significant variation in amylase-binding proteins among streptococci and that the high and low molecular mass proteins differ in the way they interact with salivary amylase.
人唾液α-淀粉酶的酶促和链球菌结合位点之间的结构关系。
DOI：
10.1016/s0006-291x(05)80900-3
发表时间：
1990
影响因子：
3.1
作者：
Scannapieco,FA;Bhandary,K;Ramasubbu,N;Levine,MJ
通讯作者：
Levine,MJ