INTERACTION OF MERCURY WITH HUMAN ERYTHROCYTES
The binding of mercury to red blood cells was measured in terms of Hg/ sup 203/ uptake and desorption. The significant features of the binding are rapid achievement of equilibrium; release of a Hg-complexing material from the red cells themselves which distorts the binding curves at low concentrations of metal; prevention of binding by cysteine, glutathione, penicillamine, and EDTA but not by imidazole or histidine; binding of mercury in amounts up to 7 times the reduced glutathione concentration of the cells before combination with glutathione itself; and 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/sup +/, and decrease in osmotic fragility. These effects increase over the range of concentrations (1 x 10/sup -17/ to 1 x 10/sup -15/ moles of Hg/RBC) well below those that result in saturation of the cellular binding sites; above 1 x 1O/sup - 15/ moles/RBC, the effects decrease as the cells become saturated. (auth)
- Research Organization:
- Univ. of Rochester, N.Y.
- NSA Number:
- NSA-16-023393
- OSTI ID:
- 4822264
- Journal Information:
- Journal of General Physiology (U.S.), Journal Name: Journal of General Physiology (U.S.) Vol. Vol: 45; ISSN JGPLA
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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