Chan M K, Minta J O
Immunopharmacology. 1985 Aug;10(1):61-7. doi: 10.1016/0162-3109(85)90060-8.
We have examined the effects of anti-inflammatory and anti-rheumatic drugs on membrane-bound and purified Na+/K+-ATPase activity in vitro. Only the gold-containing compounds (gold sodium thiomalate and auranofin) were found to inhibit the enzyme activity in a dose-dependent manner. Sodium thiomalate and triethylphosphine, the ligand compounds for gold sodium thiomalate and auranofin, respectively, had no effect on ATPase activity. The antagonistic properties was abolished by preincubation of the gold compounds with dithiothreitol. Lineweaver-Burke analysis of the inhibitions of purified ATPase by the gold compounds was found to follow uncompetitive kinetics. Inhibition of ATPase by gold may cause disruption of transmembrane cation transport and thus result in impairment of several metabolic processes and cellular functions.
我们已经在体外研究了抗炎和抗风湿药物对膜结合及纯化的Na⁺/K⁺-ATP酶活性的影响。仅发现含金化合物（硫代苹果酸金钠和金诺芬）以剂量依赖方式抑制该酶活性。硫代苹果酸钠和三乙膦分别作为硫代苹果酸金钠和金诺芬的配体化合物，对ATP酶活性没有影响。通过将金化合物与二硫苏糖醇预孵育，其拮抗特性被消除。发现金化合物对纯化ATP酶的抑制作用经Lineweaver-Burke分析呈非竞争性动力学。金对ATP酶的抑制可能导致跨膜阳离子转运的破坏，从而导致多种代谢过程和细胞功能受损。
