Fiehn N E, Moe D
Scand J Dent Res. 1983 Oct;91(5):365-70. doi: 10.1111/j.1600-0722.1983.tb00831.x.
Supragingival plaque samples were examined for alpha-amylase activity before and after cultivation. Amylase activity was determined by disappearance of 14C-labeled starch in a phosphate buffer, pH 6.9. In all plaque samples alpha-amylase activity was observed. On an average 75% of this activity was soluble, while the rest was bound to various plaque components. Known inhibitors of human alpha-amylase inhibited the enzyme activity in the plaque samples almost totally. The electrophoretic patterns of alpha-amylases in the plaque and human saliva samples were identical. Bacteria cultivated from the plaque samples showed no or low alpha-amylase activity. The results indicated that most of alpha-amylase activity in supragingival plaque samples are of salivary origin. The greater part of the enzyme activity is extracellular in the plaque, may be located at the plaque surface, and only a minor part is bound to the cells or to the insoluble components in the plaque.
在培养前后对龈上菌斑样本进行α-淀粉酶活性检测。淀粉酶活性通过在pH 6.9的磷酸盐缓冲液中14C标记淀粉的消失来测定。在所有菌斑样本中均观察到α-淀粉酶活性。平均而言，该活性的75%是可溶的，其余部分则与各种菌斑成分结合。已知的人α-淀粉酶抑制剂几乎完全抑制了菌斑样本中的酶活性。菌斑和人唾液样本中α-淀粉酶的电泳图谱相同。从菌斑样本中培养出的细菌显示无α-淀粉酶活性或活性较低。结果表明，龈上菌斑样本中大部分α-淀粉酶活性来源于唾液。该酶活性的大部分在菌斑中是细胞外的，可能位于菌斑表面，只有一小部分与菌斑中的细胞或不溶性成分结合。
