[通过蛋白激酶从大鼠嗜铬细胞瘤中共同纯化酪氨酸羟化酶]
[Copurification of tyrosine hydroxylase from rat pheochromocytoma by protein kinase].
作者信息
Pigeon D, Drissi-Daoudi R, Gros F, Thibault J
出版信息
C R Acad Sci III. 1986;302(12):435-8.
PMID:2872947
Abstract
Rat pheochromocytoma contains a protein kinase activity which remains associated with tyrosine hydroxylase (TH) during its purification. The incorporation of phosphate in TH is observed after incubation of TH with labelled ATP and magnesium without the need for an exogenous protein kinase. This Ca2+ and cAMP-independent kinase activity is different from previously described TH phosphorylating kinases from rat pheochromocytoma and other tissues.
摘要
大鼠嗜铬细胞瘤含有一种蛋白激酶活性，在其纯化过程中该活性始终与酪氨酸羟化酶（TH）相关联。将TH与标记的ATP和镁一起孵育后，可观察到TH中有磷酸盐掺入，而无需外源性蛋白激酶。这种不依赖Ca2+和cAMP的激酶活性不同于先前描述的来自大鼠嗜铬细胞瘤和其他组织的TH磷酸化激酶。
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