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The cytochemical distribution of Ca2+-Mg2+-ATPase was studied ultrastructurally, using a lead capture method at pH 8.5 and compared in various tissues. In thymic, splenic and activated peripheral blood lymphocytes and in cultured HeLa cells activity was consistently localised on the nuclear envelope, endoplasmic reticulum, Golgi apparatus, mitochondria and weakly on centrioles, but not on the plasma membrane. Intracellular activity was similarly distributed in intestinal absorptive cells where activity was particularly strong in the Golgi apparatus, and in hepatocytes where, however, activity was generally weak. Intracellular activity was lacking in renal glomerular and tubular cells and in cerebellar neurons and neuroglia. Variable activity was present on the outer surface of the plasma membrane, particularly on the brush borders of intestinal and renal tubular absorptive cells, the basolateral invaginations of distal tubules and the bile canaliculi. Mitochondrial activity, when present, was inhibited by oligomycin. The localisation at different sites may represent biochemically different ATPases including endoplasmic reticular ATPase involved in intracellular calcium regulation, oligomycin-sensitive mitochondrial ATPase, dynein-like ATPase associated with centrioles and an ectoenzyme associated with cell surface specialisations.