Quarfoth G, Ahmed K, Foster D
Biochim Biophys Acta. 1978 Oct 12;526(2):580-90. doi: 10.1016/0005-2744(78)90148-1.
Spermine and spermidine inhibit the (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) reaction so that the effect increases as the ionic content due to Na+ and K+ in the reaction is reduced. Several other amines inhibit (Na+ + K+)-ATPase to varying degress and methylglyoxal-bis-(guanylhydrazone) was the most potent inhibitor among those tested. The inhibition by polyamines of the ATPase is uncompetitive with respect to Mg2+ and ATP activation of the reaction. Various naturally occurring polyamines and other amines inhibited Na+ activation of (Na+ + K+)-ATPase as well as Na+-dependent phosphoenzyme formation in an apparently competitive manner with respect to Na+. Likewise, K+-activation of (Na+ + K+)-ATPase as well as K+-p-nitrophenyl phosphatase was inhibited in an apparently competitive manner with respect to K+. Both the cation charge and structure (e.g., aliphatic chain length) may contribute to the inhibitory effects of the amines; however, Na+ sites appear to be more sensitive to cation charge than the aliphatic chain length of the amine, whereas the opposite appears to be true for K+ sites. The results do not indicate a specific effect of polyamines on (Na+ + K+)-ATPase or its partial reactions.
精胺和亚精胺抑制（Na⁺ + K⁺）-ATP酶（ATP磷酸水解酶，EC 3.6.1.3）反应，因此随着反应中因Na⁺和K⁺导致的离子含量降低，这种抑制作用增强。其他几种胺类对（Na⁺ + K⁺）-ATP酶有不同程度的抑制作用，在测试的胺类中，甲基乙二醛双（胍腙）是最有效的抑制剂。多胺对ATP酶的抑制作用在Mg²⁺和ATP对反应的激活方面是非竞争性的。各种天然存在的多胺和其他胺类以明显竞争性的方式抑制（Na⁺ + K⁺）-ATP酶的Na⁺激活以及Na⁺依赖性磷酸酶的形成，相对于Na⁺而言。同样，（Na⁺ + K⁺）-ATP酶的K⁺激活以及K⁺-对硝基苯磷酸酶以明显竞争性的方式相对于K⁺受到抑制。阳离子电荷和结构（例如脂肪链长度）可能都对胺类的抑制作用有贡献；然而，Na⁺位点似乎对阳离子电荷比胺类的脂肪链长度更敏感，而对于K⁺位点情况似乎相反。结果并未表明多胺对（Na⁺ + K⁺）-ATP酶或其部分反应有特异性作用。
