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大鼠肝脏被膜小泡的网格蛋白β轻链在体内外均可被磷酸化。

Clathrin beta-light chain of rat liver coated vesicles is phosphorylated in vitro and in vivo.

作者信息

Cantournet B, Creuzet C, Komano O, Loeb J

出版信息

FEBS Lett. 1987 Aug 10;220(1):143-8. doi: 10.1016/0014-5793(87)80892-x.

Abstract

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.

摘要

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。

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