Hg2+ binding to ouabain-sensitive Na+-K+-ATPase of rat platelet membrane was specific with a Ka of 1.3 x 10(9) moles and Bmax of 3.8 nmoles/mg protein. The binding of mercury to Na+-K+-ATPase also inhibits the enzyme significantly (P < 0.001), which is greater than its ouabain sensitivity. Further in the cytosol of washed platelets conjugation of reduced glutathione (GSH) to Hg2+ is correlated dose dependently (25, 50 and 100 pmoles) to enhanced GSH-S-transferase (GST) activity. It may be concluded from the present in vitro experiments that mercury binds specifically to thiol groups present in the platelet membrane Na+-K+-ATPase, inhibits the enzyme and induces changes in platelet function, namely, platelet aggregation by interfering with the sodium pump.
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