PHOSPHORYLATION OF THE CATALYTIC SUBUNIT OF NA+,K+-ATPASE INHIBITS THE ACTIVITY OF THE ENZYME
PHOSPHORYLATION OF THE CATALYTIC SUBUNIT OF NA+,K+-ATPASE INHIBITS THE ACTIVITY OF THE ENZYME
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DOI：
10.1073/pnas.88.24.11359
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发表时间：
1991-12-01
影响因子：
11.1
通讯作者：
GREENGARD, P
中科院分区：
文献类型：
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作者：
BERTORELLO, AM;APERIA, A;GREENGARD, P
我们已经检测了两种不同的蛋白激酶，cAMP依赖的蛋白激酶和蛋白激酶C，以研究它们对三种不同类型的Na+，K+-ATPase制剂的磷酸化和调节活性的能力。CAMP依赖的蛋白激酶磷酸化纯化的鲨鱼直肠腺Na+，K+-ATPase，其化学计量比约为每摩尔亚单位1摩尔的磷酸盐。蛋白激酶C使纯化的鲨鱼直肠腺Na+，K+-ATPase磷酸化，其化学计量比约为每摩尔亚单位2摩尔磷酸盐。每种酶的磷酸化对Na+，K+-ATPase活性的抑制约为40-50%。这两种蛋白激酶对部分纯化的大鼠肾皮质Na~+，K~+-ATPase和大鼠肾皮质基底膜囊泡的Na~+，K~+-ATPase也有抑制作用。
We have examined two distinct protein kinases, cAMP-dependent protein kinase and protein kinase C, for their ability to phosphorylate and regulate the activity of three different types of Na+,K+-ATPase preparation. cAMP-dependent protein kinase phosphorylated purified shark rectal gland Na+,K+-ATPase to a stoichiometry of approximately 1 mol of phosphate per mol of a subunit. Protein kinase C phosphorylated purified shark rectal gland Na+,K+-ATPase to a stoichiometry of approximately 2 mol of phosphate per mol of a subunit. The phosphorylation by each of the kinases was associated with an inhibition of Na+,K+-ATPase activity of about 40-50%. These two protein kinases also inhibited the activity of a partially purified preparation of Na+,K+-ATPase from rat renal cortex and the activity of Na+,K+-ATPase present in preparations of basolateral membrane vesicles from rat renal cortex.