Braughler J M, Corder C N
Biochim Biophys Acta. 1978 Jun 9;524(2):455-65. doi: 10.1016/0005-2744(78)90184-5.
Human renal (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) preparations which exhibited a non-linear reaction rate, contained high levels of membrane-bound cyclic AMP-dependent protein kinase, while this latter activity was much less or absent in purified preparations. A non-linear reaction rate was observed in a purified preparation of (Na+ + K+)-ATPase by reconstituting the enzyme into lipid vesicles with cyclic AMP-dependent protein kinase. The addition of cyclic AMP to the ATPase assay of these lipid vesicles inactivated the (Na+ + K+)-ATPase. The cytoplasmic fraction of the cell contained a nondialyzable factor, which prevented (or reversed) the cyclic AMP-mediated inactivation of the enzyme.
具有非线性反应速率的人肾（Na+ + K+）-ATP酶（ATP磷酸水解酶，EC 3.6.1.3）制剂含有高水平的膜结合环磷酸腺苷依赖性蛋白激酶，而在纯化制剂中，后一种活性则低得多或不存在。通过将（Na+ + K+）-ATP酶与环磷酸腺苷依赖性蛋白激酶一起重构到脂质囊泡中，在（Na+ + K+）-ATP酶的纯化制剂中观察到了非线性反应速率。向这些脂质囊泡的ATP酶测定中添加环磷酸腺苷会使（Na+ + K+）-ATP酶失活。细胞的细胞质部分含有一种不可透析的因子，它可阻止（或逆转）环磷酸腺苷介导的酶失活。
