Abstract
A guinea pig kidney membrane preparation was incubated with thimerosal and then thoroughly washed. Comparison of the properties of the native and the modified membranes showed that (a) Na ++K +-dependent activity is substantially inhibited by thimerosal; (b) thimerosal does not diminish Na +-dependent ATPase activity; and (c) the thimerosal treated enzyme, like the native enzyme, is phosphorylated in the presence of Na + and ATP, and dephosphorylated upon the addition of K +. It is suggested that thimerosal does not affect the binding of ATP to the high-affinity catalytic site, but that it blocks the binding of ATP to a low affinity modifying site the occupation of which is essential for the dissociation of the stable K +-dephosphoenzyme and the recycling of the enzyme.
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