Wheeler K P, Walker J A
Biochem J. 1975 Mar;146(3):723-7. doi: 10.1042/bj1460723.
The phospholipid-dependence of the (Na-++K-+)-dependent ATPase (adenosine triphosphatase) (EC 3.6.1.3) and associated K-+-dependent phosphatase activity (EC 3.6.1.7) have been compared. Unlike the (Na-++K-+)-dependent ATPase activities, the K-+-dependent phosphatase activities of a number of different preparations were not closely correlated with their total phospholipid contents. After partial lipid depletion with a single extraction in Lubrol W the residual ATPase and phosphatase activities were correlated, but their magnitudes were quite different: on average only about 5% of the former remained compared with 50% of the latter. A similar differential effect on these activities was found after extraction with deoxycholate. In contrast with the ATPase, consistent restoration of the phosphatase activity of Lubrol-extracted enzymes by added exogenous phospholipids was not observed. We conclude that, although the K-+-dependent phosphatase may be lipid-dependent, the lipid requirement must be different from that of the complete ATPase system, and this difference should help investigations of their relationship.
对（Na⁺+K⁺）依赖的ATP酶（腺苷三磷酸酶）（EC 3.6.1.3）以及相关的K⁺依赖的磷酸酶活性（EC 3.6.1.7）的磷脂依赖性进行了比较。与（Na⁺+K⁺）依赖的ATP酶活性不同，许多不同制剂的K⁺依赖的磷酸酶活性与其总磷脂含量没有密切相关性。用Lubrol W单次提取进行部分脂质去除后，残留的ATP酶和磷酸酶活性具有相关性，但它们的大小差异很大：前者平均仅保留约5%，而后者保留50%。用脱氧胆酸盐提取后，对这些活性也发现了类似的差异效应。与ATP酶相反，未观察到通过添加外源性磷脂使Lubrol提取的酶的磷酸酶活性持续恢复。我们得出结论，虽然K⁺依赖的磷酸酶可能依赖脂质，但其脂质需求一定不同于完整的ATP酶系统，这种差异应有助于对它们之间关系的研究。
