Interaction of di- and tributyltin chloride with human erythrocyte membrane.

Analysis of the binding of tributyltin chloride (TBT) to human erythrocyte membrane indicated a single class of binding site with an affinity of approximately 6.78 X 10(3) M-1, whereas dibutyltin dichloride (DBT) showed the presence of more than one class of binding sites with a high affinity value of 2.53 X 10(4) M-1 and a low affinity value of 2.06 X 10(3) M-1. Membrane protein binding studies revealed that both di- and tributyltin compounds bind significantly with band 3 protein of the erythrocyte membrane. These results indicate the significant interactions of erythrocyte membrane components with alkyltin compounds.