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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Inorganic mercury interacts with thiols at the nucleotide and cationic binding sites of the ouabain-sensitive cerebral electrogenic sodium pump
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Inorganic mercury interacts with thiols at the nucleotide and cationic binding sites of the ouabain-sensitive cerebral electrogenic sodium pump

机译：无机汞与哇巴因敏感性脑电钠泵的核苷酸和阳离子结合位点上的硫醇相互作用

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摘要

The molecular events leading to neuronal dysfunction often associated with mercury toxidty can be complex and is yet to be fully elucidated. Hence, the present study sought to evaluate the interaction of inorganic mercury (Hg~(2+)) with the ouabain-sensitive electrogenic pump in partially purified mammalian brain membrane preparations. The results show that Hg~(2+) significantly inhibited the transmembrane enzyme in a concentration dependent manner. In addition, Hg~(2+) exerts its inhibitory effect on the activity of the enzyme by interacting with groups at the adenosine triphosphate (ATP), Na~+ and 10" binding sites. However, preincubation of the enzyme with exogenous monothiols, cysteine, prevented the inhibition of Hg~(2+) on the pump's activity suggesting that Hg~(2+) may be interacting with the thiols at the nucleotide (ATP) and cationic (Na~+ and K~+) binding sites. In fact, our data show that Hg~(2+) oxidizes sulphydryl groups in cysteine in a time dependent fashion in vitro. Finally, we speculate that the small molecular volume of Hg~(2+) in comparison with the substrates (ATP, Na~+ and K~+) of sodium pump, its possibly high reactivity and strong affinity for thiols may account for its high toxicity towards the membrane bound ouabain-sensitive electrogenic pump.
机译：经常与汞氧化有关的导致神经元功能障碍的分子事件可能很复杂，尚待充分阐明。因此，本研究试图评估部分纯化的哺乳动物脑膜制剂中无机汞（Hg〜（2+））与哇巴因敏感的电泵之间的相互作用。结果表明，Hg〜（2+）以浓度依赖的方式显着抑制跨膜酶。此外，Hg〜（2+）通过与三磷酸腺苷（ATP），Na〜+和10“结合位点上的基团相互作用，对酶的活性产生抑制作用。但是，将酶与外源性单硫醇预温育，半胱氨酸阻止了Hg〜（2+）对泵的活性的抑制，表明Hg〜（2+）可能在核苷酸（ATP）和阳离子（Na〜+和K〜+）结合位点与硫醇相互作用。实际上，我们的数据表明，Hg〜（2+）在体外以时间依赖性方式氧化半胱氨酸中的巯基，最后，我们推测Hg〜（2+）与底物（ATP，钠泵的Na〜+和K〜+）可能具有较高的反应性和对硫醇的强亲和力，可能是其对与膜结合的哇巴因敏感的电泵产生的高毒性。

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