The inhibition of (Na+-K+)-activated ATPase by beryllium.
The inhibition of (Na+-K+)-activated ATPase by beryllium.
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铍对 (Na -K ) 激活的 ATP 酶的抑制。
DOI：
10.1016/0005-2736(67)90049-1
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发表时间：
1967
期刊：
影响因子：
--
通讯作者：
S. Minakami
中科院分区：
文献类型：
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作者：
G. Toda;T. Hashimoto;T. Asakura;S. Minakami
据报道，铍抑制碱性磷酸酶（EC 3.1。3.1)通过与Mg 2+竞争（参考文献10），第1-4段）。磷酸葡萄糖变位酶（EC 2.7. 5.1)由于已知许多二价阳离子对Na ~+-K ~+ ATP酶6具有抑制作用，因此我们计划研究铍对该酶的影响。在我们的研究过程中，托马斯和阿尔德里奇7报道了相当高浓度的BeSOt（0.64 mM）对脑微粒体ATP酶的抑制作用。他们描述了这种抑制作用是由于铍与ATP的结合，从而耗尽了酶中通常的Mg 2 +-ATP复合物。他不认为这种抑制作用是由于铍对酶的直接作用。然而，我们发现铍对豚鼠肾皮质微粒体Na ~+-K ~+ ATP酶的抑制作用还依赖于Na ~+、K ~+和Mg 2~+等阳离子的存在。实验结果表明，铍对酶的抑制作用是由于铍对酶的直接作用，而Na+、K+和Mg 2+在无ATP存在时改变了酶的状态。从豚鼠肾皮质和肾皮质制备微粒体ATP酶，
It has been reported that beryllium inhibits alkaline phosphatase (EC 3.1. 3.1) by competing with Mg 2+(refs. 1-4). Phosphoglucomutase (EC 2.7. 5.1) is found to be irreversibly inhibited by binding a mole of beryllium per mole of enzyme, presumably to Mg"+ site 5.Since many divalent cations are known to be inhibitory to Na+-K+ ATPase 6, we planned to study the effect of beryllium on this enzyme. During the course of our study, THOMAS AND ALDRIDGE 7 reported on the inhibition of brain microsomal ATPase by rather high concentration of BeSOt (0.64 mM). They described the inhibition to be due to a combination of beryllium with ATP, thereby depleting the enzyme of its usual Mg2+-ATP complex. He did not consider the inhibition to be due to the direct action of beryllium on the enzyme. We found, however, beryllium inhibition of Na+-K+ ATPase prepared from microsomal fraction of guinea-pig kidney cortex to be additionally dependent on the presence of cations such as Na+, K+, and Mg 2~. The data described below suggest that the inhibition is due to the direct action of beryllium on the enzyme and that Na÷, K+ arid Mg 2+ change the state of the enzyme in the absence of ATP. Microsomal ATPase was prepared from'guinea-pig kidney cortex s and care-