Abstract
A specific inhibitor of SERCA-pumps, thapsigargin (TG) was used to demonstrate the direct involvement of the SR Ca 2+-ATPase in passive K +/Na + exchange. The K +-potential variations across vesicle membranes were measured in the absence of ATP with a fluorescent probe: 3,3′-dipropylthiodicarbocyanine iodide. Addition of EGTA dissipates the K +-potential whereas the presence of TG abolishes this effect. Our data prove that the Ca 2+-ATPase translocates monovalent cations at a rate similar to the E 2→E 1 conformational change.
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