Sjögren S, Persson B, Hammarström L
Acta Odontol Scand. 1986 Jun;44(3):177-84. doi: 10.3109/00016358609026571.
Alkaline phosphatases (AlkPase) of many different tissues and species have been shown to be zinc metalloenzymes. Specific regions of rat oral mucosa have a high activity of AlkPase. Combined autoradiography and enzyme histochemistry showed that they also retained injected radioactive zinc (65Zn). The AlkPase activity was inactivated by EDTA and reactivated with zinc. However, it could not be verified by polyacrylamide gel electrophoresis combined with radioactivity measurements and enzyme analysis that the 65Zn uptake of oral mucosa was incorporated in the AlkPase molecule.
许多不同组织和物种的碱性磷酸酶（AlkPase）已被证明是锌金属酶。大鼠口腔黏膜的特定区域具有较高的AlkPase活性。放射自显影和酶组织化学相结合表明，它们还保留了注入的放射性锌（65Zn）。AlkPase活性被EDTA灭活并被锌重新激活。然而，通过聚丙烯酰胺凝胶电泳结合放射性测量和酶分析，无法证实口腔黏膜对65Zn的摄取被纳入了AlkPase分子中。
