Cantournet B, Creuzet C, Komano O, Loeb J
FEBS Lett. 1987 Aug 10;220(1):143-8. doi: 10.1016/0014-5793(87)80892-x.
Clathrin beta-light chain of rat liver coated vesicles is phosphorylated in vitro in the presence of poly(L-lysine) by an endogenous protein kinase which appears to be similar to casein kinase II. Clathrin beta-light chain is also phosphorylated in vivo. After injection of [32P]phosphate into rats and preparation of purified coated vesicles in the presence of phosphatase inhibitors, electrophoretic analysis showed the presence of several labeled polypeptides including clathrin beta-light chain. A polypeptide of 50 kDa, which may correspond to the major polypeptide phosphorylated in vitro of coated vesicles, is also labeled in vivo.
大鼠肝脏被膜小泡的网格蛋白β轻链，在聚（L-赖氨酸）存在的情况下，可被一种内源性蛋白激酶在体外磷酸化，该激酶似乎与酪蛋白激酶II相似。网格蛋白β轻链在体内也会被磷酸化。向大鼠注射[32P]磷酸盐并在磷酸酶抑制剂存在的情况下制备纯化的被膜小泡后，电泳分析显示存在几种标记多肽，包括网格蛋白β轻链。一种50 kDa的多肽，可能对应于体外被膜小泡中主要的磷酸化多肽，在体内也被标记。
