Tokuda M, Khanna N C, Arora A K, Waisman D M
Biochem Biophys Res Commun. 1986 Sep 30;139(3):910-7. doi: 10.1016/s0006-291x(86)80264-9.
High levels of tyrosine protein kinase have been recently detected in the membranes of rat spleen. In the present report the tyrosine protein kinase activity of the 30,000 x g pellet of rat spleen has been solubilized and partially purified by ion exchange and gel permeation chromatography. Two peaks of tyrosine protein kinase of Mr 35,000 (TPK-I) and Mr 40,000 (TPK-II) have been resolved. These kinases were free of the EGF receptor and insulin receptor tyrosine protein kinases. Although TPK-I and TPK-II phosphorylated angiotensin II, casein, histone, tubulin, phosphorylase b, and p36 they differed from each other in preference for the substrates. Both tyrosine protein kinases did not phosphorylate anti-pp60v-src IgG.
最近在大鼠脾脏细胞膜中检测到高水平的酪氨酸蛋白激酶。在本报告中，大鼠脾脏30,000×g沉淀的酪氨酸蛋白激酶活性已通过离子交换和凝胶渗透色谱法溶解并部分纯化。已分离出分子量为35,000（TPK-I）和40,000（TPK-II）的两个酪氨酸蛋白激酶峰。这些激酶不含表皮生长因子受体和胰岛素受体酪氨酸蛋白激酶。尽管TPK-I和TPK-II使血管紧张素II、酪蛋白、组蛋白、微管蛋白、磷酸化酶b和p36磷酸化，但它们对底物的偏好不同。两种酪氨酸蛋白激酶均未使抗pp60v-src IgG磷酸化。
