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组织匀浆中汞结合情况的研究。

Studies on the binding of mercury in tissue homogenates.

作者信息

Clarkson T W, Magos L

出版信息

Biochem J. 1966 Apr;99(1):62-70. doi: 10.1042/bj0990062.

Abstract
  1. This paper describes an attempt to learn more about the binding of Hg(2+) to tissues at pharmacological concentrations of this metal. Other methods were not applicable to such low concentrations of mercury. 2. The method involved equilibrium dialysis of Hg(2+) against 1% homogenates of rat kidney or liver in the presence of penicillamine. Two classes of mercury-binding sites were observed, one class having a chemical affinity for mercury 100-fold greater than the other class. The binding capacities of the class of higher and lower affinity were respectively 1.0x10(-7) and 30x10(-7)mole of mercury/g. wet wt. of tissue. The same classes of binding sites were found in both liver and kidney homogenates. 3. The binding sites of both classes reacted with only one valency of Hg(2+), the other valency forming a bond with penicillamine. Thus the total binding capacities of both classes are equivalent to 50% of the total reactive protein-bound thiol groups in the homogenate. 4. The results eliminate three possible mechanisms for the preferential accumulation of mercury by kidney. They support the idea that the permeability changes in kidney cells resulting in diuresis are similar to the permeability changes produced on the membranes of other mammalian cell species by mercury.
摘要
  1. 本文描述了一项旨在更深入了解在该金属的药理浓度下汞离子(Hg(2+))与组织结合情况的尝试。其他方法不适用于如此低浓度的汞。2. 该方法涉及在青霉胺存在的情况下,将Hg(2+)与大鼠肾脏或肝脏的1%匀浆进行平衡透析。观察到两类汞结合位点,一类对汞的化学亲和力比另一类高100倍。高亲和力和低亲和力类别的结合容量分别为1.0×10⁻⁷和30×10⁻⁷摩尔汞/克组织湿重。在肝脏和肾脏匀浆中均发现了相同类别的结合位点。3. 两类结合位点均仅与Hg(2+)的一个价态反应,另一个价态与青霉胺形成键。因此,两类的总结合容量相当于匀浆中总反应性蛋白质结合巯基的50%。4. 这些结果排除了肾脏优先积累汞的三种可能机制。它们支持这样一种观点,即导致利尿的肾细胞通透性变化类似于汞对其他哺乳动物细胞种类膜产生的通透性变化。

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本文引用的文献

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Protein mercaptides.蛋白质硫醇盐
Cold Spring Harb Symp Quant Biol. 1950;14:79-84. doi: 10.1101/sqb.1950.014.01.011.
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Interaction of mercury with human erythrocytes.汞与人体红细胞的相互作用。
J Gen Physiol. 1962 Jan;45(3):395-410. doi: 10.1085/jgp.45.3.395.

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