CYTOCHEMICAL LOCALIZATION OF MG^<++>-ATPASE AND CA^<++>-ATPASE ON THE LIMITING MEMBRANE OF RAT LIVER PEROXISOMES

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By a modified cytochemical staining procedure, Mg^<++>- and Ca^<++>-ATPase were clearly localized on the surface of the limiting membrane of peroxisomes in hepatocytes of the rat. The matrix and core structure (crystalloid) were devoid of the ATPase reaction. The reaction on the peroxisomal membrane was abolished by an inhibitor of Mg^<++>-ATPase, 10 mM p-chloromercuric benzoate (PCMB) and by the omission of the substrate, ATP-2Na, or by replacement of it with β-glycerophosphate. The reaction was not suppressed by the inhibitor of a alkaline phosphatase, 2.5 mM levamisole; by an inhibitor of Na-K-ATPase, 10 mM ouabain. After replacement of MgSO_4 by CaCI_2, Ca-ATPase was localized at exactly the same site where Mg-ATPase was detected.
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