Gonçalves de Moraes V L, De Meis L
Biochim Biophys Acta. 1982 May 21;688(1):131-7. doi: 10.1016/0005-2736(82)90587-9.
(Na+,K+)-ATPase is able to catalyze a continuous ATP in equilibrium Pi exchange in the presence of Na+ and in the absence of a transmembrane ionic gradient. At pH 7.6 the Na+ concentration required for half-maximal activity is 85 mM and at pH 5.1 it is 340 mM. In the presence of optimal Na+ concentration, the rate of exchange is maximal at pH 6.0 and varies with ADP and Pi concentration in the assay medium. ATP in equilibrium Pi exchange is inhibited by K+ and by ouabain.
(钠钾)-ATP 酶能够在有 Na⁺且无跨膜离子梯度的情况下催化持续的 ATP 与 Pi 的平衡交换。在 pH 7.6 时,达到最大活性一半所需的 Na⁺浓度为 85 mM,在 pH 5.1 时为 340 mM。在存在最佳 Na⁺浓度的情况下,交换速率在 pH 6.0 时最大,并且随测定介质中 ADP 和 Pi 的浓度而变化。ATP 与 Pi 的平衡交换受到 K⁺和哇巴因的抑制。