糖原合成酶激酶３（ Ｇ Ｓ Ｋ３）在 ３０℃与 τ蛋白保温 ４ ｈ 可催化 １７±０４ ｍ ｏｌ磷酸参入 １ ｍ ｏｌτ蛋白 将磷酸化的 τ蛋白经胰蛋白酶消化， Ｆｅ Ｃｌ３ 亲和柱分离及 Ｃ１８反相高压液相层析纯化后，再用高压电泳，手工 Ｅｄｍ ａｎ 降解及自动氨基酸序列分析等检测技术，对其磷酸化位点进行鉴定 结果发现： Ｇ Ｓ Ｋ３ 可使 τ蛋白 Ｔｈｒ１８１， Ｓｅｒ１８４， Ｓｅｒ２６２， Ｓｅｒ３５６ 和 Ｓｅｒ４００ 发生磷酸化 其中 Ｓｅｒ２６２ 和 Ｓｅｒ４００ 为 Ａｌｚｈｅｉｍ ｅｒ 病（ Ａ Ｄ）τ蛋白的异常磷酸化位点根据上述磷酸化作用仅轻度抑制τ蛋白生物学活性，推测： Ａ Ｄ τ蛋白 Ｓｅｒ２６２ 和 Ｓｅｒ４００ 的磷酸化可能不是决定其生物功能的关键性位点，单纯 Ｇ Ｓ Ｋ３ 不能复制 Ａ Ｄ 样 τ蛋白的病理改变  Glycogen synthase kinase  3 (G S K3) incubated with tau protein for 4 h at 30 ℃ catalyzed 1  7 ± 04 m ol phosphate into 1 m ol 蛋 protein. The phosphorylated tau protein was activated by trypsin Digestion, Fe Cl3 affinity column and C18 reversed-phase high pressure liquid chromatography purification, and then high-pressure electrophoresis, manual Edm an degradation and automatic amino acid sequence analysis of detection techniques to identify its phosphorylation site found  found: G S K 3 can make the tau protein Thr181, Ser184, Ser266, Ser356 and Ser400 phosphorylation which Ser262 and Ser400 is Alzheimer’s disease (AD) tau protein According to the above phosphorylation, it only slightly inhibits the biological activity of tau protein. It is speculated that the phosphorylation of Ser-262 and Ser-400 of A D Tau may not be the key site to determine its biological function, Simple G S A D 3 not replicate like protein τ pathology 