title: Separation of rat liver lysosome membrane adenosine triphosphatase activities by polyacrylamide gel electrophoresis.
abstract: Solubilization of rat liver lysosome membranes with octyl glucoside or lauryl sarcosinate and analysis of ATPase activities in sections of polyacrylamide gels after electrophoresis revealed one major peak at pH 8 and two peaks at pH 5. The pH 8 ATPase peak was not localized in the same peak with pH 5 ATPase activity, suggesting that these were catalyzed by different proteins. Ca2+- and Mg2+-ATPase activities at pH 8 were present in the same major peak, with Ca2+ activity predominating. The pH 8 Ca2+-ATPase was also not present in the same area of the gels as Ca2+-ADPase.
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000378:metabolism; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005960:Glucosides; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D051381:Rats; D012521:Sarcosine / Q000031:analogs & derivatives; D012995:Solubility
chemical_list: D005960:Glucosides; C018619:octyl-beta-D-glucoside; C025231:sarkosyl; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D012521:Sarcosine