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  • Binding of TRIETHYLLEAD CHLORIDE (cas 1067-14-7) by hemoglobin
  • Add time:07/24/2019         Source:sciencedirect.com

    The interaction of TRIETHYLLEAD CHLORIDE (cas 1067-14-7) with human and rat hemoglobin has been investigated using equilibrium dialysis. In addition the uptake of triethyllead by washed human and rat erythrocytes has been studied in vitro and the distribution of the organolead between blood cells and plamsa has been examined in vivo in the rat. Total lead was determined to atomic absorption spectrophotometry. Equilibrium dialysis demonstrated that human hemoglobin had a very low affinity and capacity for the binding of triethyllead. On the other hand, each tetramer of rat hemoglobin bound 3 mol of triethyllead at sites which did not exhibit cooperativity. ATP, EDTA, Na2S, and NaNO2 had no effect on the binding of triethyllead by rat hemoglobin while urea, glutathione, and N-ethylmaleimide inhibited the interaction. Rat red cells took up more triethyllead than did human red cells and the difference was not due to a higher binding capacity of the rat cell membrane for the organometal. For 80 min following the intravenous injection of triethyllead chloride, the total blood lead in rats was about 10 times the total plasma lead. It was concluded that triethyllead binds to the globin moiety of rat hemoglobin and that organometal binding sites occur on the hemoglobin tetramer but not on the monomers. The results demonstrated that the binding of triethyllead to hemoglobin is a significant determinant of the pharmacokinetics of the organometal in the rat and that the interaction between triethyllead and human hemoglobin would not have a significant effect on the pharmacokinetics of the organometal in the human.

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