title: Acid phosphatase from liver of the frog Rana esculenta, separation and partial characterization of multiple forms.
abstract: 1. Acid phosphatase (AcPase) from liver of the frog, Rana esculenta has been isolated and purified. The enzyme is heterogeneous, showing 4 activity zones on disc electrophoresis. The AcPase was separated into 3 peaks on DEAE-cellulose. Peak A corresponding to the electrophoretic AcPase IV represents an extensively purified enzyme form. 2. The separated enzyme forms are change isomers with a molecular weight of about 33,000. They differ markedly in substrate requirements and sensitivity towards activators and inhibitors. All of them are highly activated by dithiothreitol, show a rather restricted substrate specificity, and marked activity against ATP.
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D000818:Animals; D001001:Anura; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011893:Rana esculenta / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D000135:Acid Phosphatase