Wadström T, Nord C E, Kjellgren M
Scand J Dent Res. 1976 Jul;84(4):234-9. doi: 10.1111/j.1600-0722.1976.tb00485.x.
Human salivary proteins were separated by isoelectric focusing on polyacrylamide gel in flat beds at 1000 V for 40 min. Amylase activity was detected after immersing the gel in 0.4 M tris-HCI buffer pH 7.4 to equilibrate the pH gradient. The enzyme activity was detected after diffusion into an overlayer of agarose gel containing an insoluble dye-starch polymer (Phadebas). Both whole human saliva and parotid saliva from 15 different persons contained four amylase components, except in three cases where only three bands were detected. The bands were all focused within a rather narrow pH range (pH 5.4-7.2) and the results were very reproducible.
通过在平板聚丙烯酰胺凝胶上进行等电聚焦，在1000V下电泳40分钟来分离人唾液蛋白。将凝胶浸入pH 7.4的0.4M三羟甲基氨基甲烷 - 盐酸缓冲液中以平衡pH梯度后，检测淀粉酶活性。在扩散到含有不溶性染料 - 淀粉聚合物（Phadebas）的琼脂糖凝胶覆盖层中后检测酶活性。来自15个不同人的全唾液和腮腺唾液均含有四种淀粉酶成分，但有三例仅检测到三条带。这些条带都聚焦在相当窄的pH范围内（pH 5.4 - 7.2），并且结果具有很高的重复性。
