Swann A C, Albers R W
Biochim Biophys Acta. 1981 Jun 9;644(1):36-40. doi: 10.1016/0005-2736(81)90055-9.
Effects of temperature on the Na+-dependent ADP-ATP exchange and the p-nitrophenylphosphatase reactions catalysed by (Na+, K+)-ATPase were examined. Apparent Mg2+ affinity decreased with decreasing temperature. Arrhenius plots of p-nitrophenylphosphatase in the presence of Na+ and ATP had discontinuities similar to those previously reported for (Na+ + K+)-ATPase, while those of p-nitrophenylphosphatase measured without Na+ or ATP did not. The apparent activation energy for p-nitrophenylphosphatase was a function of the physical characteristics of the cation acting at the K+ site.
研究了温度对由(Na⁺,K⁺)-ATP 酶催化的 Na⁺依赖性 ADP-ATP 交换和对硝基苯磷酸酶反应的影响。随着温度降低,表观 Mg²⁺亲和力下降。在 Na⁺和 ATP 存在下,对硝基苯磷酸酶的阿伦尼乌斯曲线具有与先前报道的(Na⁺ + K⁺)-ATP 酶类似的不连续性,而在没有 Na⁺或 ATP 的情况下测定的对硝基苯磷酸酶的阿伦尼乌斯曲线则没有。对硝基苯磷酸酶的表观活化能是作用于 K⁺位点的阳离子物理特性的函数。