title: [The effect of substrates on stability of firefly luciferase, embedded in phosphatidylcholine liposomes].
abstract: The effects of substrates (ATP and luciferin) on stability of firefly luciferase embedded into phosphatidylcholine liposomes have been studied. Luciferin did not exert any appreciable influence on enzyme inactivation. Minor concentrations of adenosine 5'-triphosphate destabilized the enzyme; however, the increase in ATP concentration markedly stabilized the enzyme entrapped into liposomes. A kinetic scheme of ATP action on enzyme inactivation is proposed. According to this scheme, the enzyme has two ATP-binding sites.
authors: A F
authors: AF
authors: Dukhovich
authors: V M
authors: VM
authors: Morozov
authors: N N
authors: NN
authors: Ugarova
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001517:Coleoptera / Q000201:enzymology*; D004795:Enzyme Stability; D007700:Kinetics; D008081:Liposomes; D008156:Luciferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010713:Phosphatidylcholines
chemical_list: D008081:Liposomes; D010713:Phosphatidylcholines; D000255:Adenosine Triphosphate; D008156:Luciferases
vernacular_title: Vliianie substratov na stabil'nost' liutsiferazy svetliakov, vstroennoĭ v liposomy iz fosfatidilkholina.