Inhibition of adenosine triphosphatases by gold.
Inhibition of adenosine triphosphatases by gold.
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金对三磷酸腺苷酶的抑制作用。
DOI：
10.1002/art.1780230409
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发表时间：
1980
影响因子：
--
通讯作者：
B. R. Nechay
中科院分区：
文献类型：
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作者：
B. R. Nechay
本文研究了氯金酸（Au ~（3+））和硫代苹果酸金钠（Au ~+）对狗脑、肾和人肾酶制剂中腺苷三磷酸酶（ATP酶）的抑制作用。Au ~（3+）对哇巴因敏感的（Na ~+ + K ~+依赖的）ATP酶和哇巴因不敏感的（Mg ~（2+）依赖的）ATP酶无差别地产生影响，其50%抑制浓度（I_（50））约为10（-6）M。Au ~（3+）对Na ~+ + K ~+ ATP酶的I_（50）在匀浆中比在微粒体组分中高几倍。酶被牛血清白蛋白保护。虽然Au ~（3+）和Au ~+对Mg ~（2+）ATP酶的抑制作用相当，但Au ~+对Na ~+ + K ~+ ATP酶的抑制作用是Au ~（3+）的2 ~ 3倍。抗坏血酸可增强Au ~（3+）的抑制作用（但不增强Au ~+），表明抗坏血酸可将Au ~（3+）还原为Au ~+。改变NaCl、KCl、MgCl 2、ATP和MgATP的浓度对Au 3+或Au+对Na+ + K+ ATP酶的抑制程度没有影响。将pH从8.0降低到6.8增强了Au+和Au 3+的抑制作用。我们的结论是，金是最有效的非特异性的Na+ + K+ ATP酶，该酶系统的其他金属抑制剂的特性不同。
Inhibition of adenosine triphosphatase (ATPase) by chlorauric acid (Au3+) and gold sodium thiomalate (Au+) was studied in dog brain and kidney and in human kidney enzyme preparations. Au3+ indiscriminately affected ouabain-sensitive (Na+ + K+-dependent) ATPase and ouabain-insensitive (Mg2+-dependent) ATPase with concentrations for 50% inhibition (I50) approximately 10(-6) M. The I50 of Au3+ for Na+ + K+ ATPase was several-fold higher in homogenates than in microsomal fractions. The enzyme was protected by bovine serum albumin. Although Au3+ and Au+ were equipotent against Mg2+ ATPase, Au+ inhibited Na+ + K+ ATPase 2 to 3 times more effectively than did Au3+. The inhibitory action of Au3+ (but not Au+) was potentiated by ascorbic acid, suggesting reduction of Au3+ to Au+ by ascorbic acid. The fractional inhibition of Na+ + K+ ATPase by Au3+ or Au+ was not affected by changing concentrations of NaCl, KCl, MgCl2, ATP, and MgATP. Decreasing pH from 8.0 to 6.8 enhanced both Au+ and Au3+ inhibition. We conclude that gold is one of the most potent nonspecific of Na+ + K+ ATPase, with characteristics differing from other metallic inhibitors of this enzyme system.