Takahashi M, Tomizawa K, Sato K, Ohtake A, Omori A
Mitsubishi Kasei Institute of Life Sciences (Project 2), Tokyo, Japan.
FEBS Lett. 1995 Sep 18;372(1):59-64. doi: 10.1016/0014-5793(95)00955-9.
During purification of tau protein kinase I and II from the bovine brain extract, a new tau protein kinase was detected and purified with phosphocellulose, gel filtration, S-Sepharose and AF-Heparin column chromatography. The molecular mass of the enzyme was determined to be 32 kDa by gel filtration and activity staining on SDS-PAGE. The enzyme is a Ser/Thr protein kinase phosphorylating tau, beta-tubulin, MAP2 and alpha-casein. Employing many synthetic peptides, the recognition site of this enzyme appears to be -SR-. The enzyme requires no second messenger and is inhibited with high concentration of heparin, but not by inhibitors of CKI. These results indicate that this enzyme, tau-tubulin kinase is novel and distinct from TPKI, II and CKI, II.
在从牛脑提取物中纯化tau蛋白激酶I和II的过程中，检测到一种新的tau蛋白激酶，并通过磷酸纤维素、凝胶过滤、S-Sepharose和AF-肝素柱色谱法进行了纯化。通过凝胶过滤和SDS-PAGE上的活性染色，确定该酶的分子量为32 kDa。该酶是一种Ser/Thr蛋白激酶，可磷酸化tau、β-微管蛋白、MAP2和α-酪蛋白。使用多种合成肽，该酶的识别位点似乎是-SR-。该酶不需要第二信使，并且会被高浓度的肝素抑制，但不会被CKI的抑制剂抑制。这些结果表明，这种酶，即tau-微管蛋白激酶是新的，与TPKI、II和CKI、II不同。
