Synaptosomes isolated from the electric organ of Torpedo marmorata contain activity of an ATPase which is located at the extracellular face of the plasma membrane. Ecto-ATPase activity can be stimulated independently and to a similar extent by either Ca-2+ or Mg-2+. Apparent Km-values for ATP are 79 microM and 53 microM for Ca-2+ and Mg-2+ respectively. Apparent Km-values for Ca-2+ and Mg-2+ at 1 mM ATP are 0.71 mM and 0.61 mM respectively. The enzyme is also activated by Mn-2+ and GTP can replace ATP as a substrate. Presence of 5'- nucleotidase activity suggests that adenosine is the final hydrolysis product. Thus hydrolysis of nucleotides released during exocytosis of synaptic vesicle contents and purine salvage must be a major role of this ecto-enzyme. We furthermore suggest that the ecto-ATPase may provide the key to understanding the storage of the high energy compound ATP in cholinergic synaptic vesicles. On depolarization of the nerve terminal and exocytosis, ATP represents the signal for activating the ATPase whereby concentrations of Ca-2+ and Mg-2+ are already saturating. Following depolarization induced Ca-2+ influx, a possible function of the ATPase may be the outward transport of Ca-2+ from the nerve terminal.