Effect of ⁵⁴Mn and Lead Interaction on their Binding with Tissue Proteins: In Vitro Studies

Abstract

The effect of ⁵⁴Mn and lead (Pb) interaction on their binding with various tissue proteins have been investigated. Pb was found to bind with low molecular weight glycoprotein in liver, brain and serum. The interaction of ⁵⁴Mn+ Pb with the proteins in serum, liver and brain resulted in increased binding of both the metals, in comparison with that observed in the presence of either metal alone. Polyacrylamide gel electrophoresis patterns of serum, liver and brain pro-teins interacted with ⁵⁴Mn+ Pb showed two distinct bands, one corresponding to ⁵⁴Mn binding protein and the other to lead binding protein. There appears to be no competition of ⁵⁴Mn and Pb for common binding sites, however, their combi-nation altered the affinity of tissue proteins to bind ⁵⁴Mn and Pb, the mechanism of which remains to be clarified.