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. 1962 Jan 1;45(3):395–410. doi: 10.1085/jgp.45.3.395

Interaction of Mercury with Human Erythrocytes

R Weed 1, J Eber 1, A Rothstein 1
PMCID: PMC2195179  PMID: 14005533

Abstract

The binding of mercury to red blood cells was measured in terms of Hg203 uptake and desorption. The significant features of the binding are: (a) rapid achievement of equilibrium (3 to 5 minutes); (b) release of a Hg-complexing material from the red cells themselves which distorts the binding curves at low concentrations of metal (2.5 x 10-7 to 5.0 x 10-6 M); (c) prevention of binding by cysteine, glutathione, penicillamine, and EDTA but not by imidazole or histidine; (d) binding of mercury in amounts up to 7 times the reduced glutathione concentration of the cells before combination with glutathione itself; (e) binding primarily to sulfhydryl groups of hemoglobin and to a small number of stromal sulfhydryl groups, but also to other non-sulfhydryl cellular ligands after saturation of the sulfhydryl groups. Associated with the binding is inhibition of glucose uptake, induction of loss of K+, and decrease in osmotic fragility. These effects increase over the range of concentrations (1 x 10-17 to 1 x 10-15 moles of Hg/RBC) well below those that result in saturation of the cellular binding sites; above 1 x 10-15 moles/RBC, the effects decrease as the cells become saturated.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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