title: Acid ATPase from chicken liver lysosomes. II. Presence of metal ion-activated enzyme.
abstract: Metal ion-activated acid ATPase was present in chicken liver lysosomes. The enzyme catalyzed the hydrolysis of nucleoside tri-, di-, and monophosphates and cleaved the phosphodiester linkage. Among the substrates studied, ATP was hydrolyzed at the highest rate at pH 5.4. The enzyme activity was stimulated 3.5 approximately 7.5-fold by divalent cations such as Ca2+, Mg2+, and Zn2+, but inhibited by EDTA or Hg2+.
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D002645:Chickens; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D000251:Adenosine Triphosphatases