Characterization of partially purified cytosolic protein-tyrosine kinase from porcine spleen.
Characterization of partially purified cytosolic protein-tyrosine kinase from porcine spleen.
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来自猪脾的部分纯化的胞质蛋白酪氨酸激酶的表征。
DOI：
10.1016/s0006-291x(88)80401-7
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发表时间：
1988
影响因子：
3.1
通讯作者：
H. Yamamura
中科院分区：
文献类型：
--
作者：
K. Sakai;S. Nakamura;K. Sada;T. Kobayashi;H. Uno;H. Yamamura
从猪脾中部分纯化了胞浆蛋白酪氨酸激酶（CPTK-40），并与牛胸腺胞浆蛋白酪氨酸激酶p40进行了比较。当CPTK-40与McCl_2和（γ-~（32）p）ATP共同孵育时，只观察到一个分子量为40千道尔顿的磷蛋白。CPTK-40以0.5nmol/min/mg的速率有效磷酸化微管蛋白。与p40激酶不同，酪蛋白也是CPTK-40的底物。在所测试的各种二价阳离子中，Co 2+、Mn 2+和Mg 2+是对酶活性有效的金属离子。Ca ~（2+）也可作为二价阳离子参与酶的活性，但速率较低。这些结果表明CPTK-40与p40激酶相似但不相同。
Biochemical properties of a cytosolic protein-tyrosine kinase (CPTK-40) partially purified from porcine spleen were characterized and compared with p40 kinase, a cytosolic protein-tyrosine kinase from bovine thymus. When CPTK-40 was incubated with McCl2and (γ-32p)ATP, only a phosphoprotein with a molecular weight of 40 kilodalton was observed. CPTK-40 efficiently phosphorylated tubulin with the rate of 0.5 nmol/min/mg. Unlike p40 kinase, casein was also a substrate for CPTK-40. Among various divalent cations tested, Co2+, Mn2+and Mg2+were effective metal ions for the enzyme activity. Ca2+could also serve as a divalent cation for the activity although the rate was low. These results suggests that CPTK-40 is similar but not identical to p40 kinase.
牛胸腺蛋白酪氨酸激酶的纯化和表征。
DOI：
--
发表时间：
1986
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Zioncheck,TF;Harrison,ML;Geahlen,RL
通讯作者：
Geahlen,RL
T 和 B 淋巴细胞表达不同的酪氨酸蛋白激酶。
DOI：
--
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Harrison,ML;Low,PS;Geahlen,RL
通讯作者：
Geahlen,RL