title: Cl anion-dependent Mg-ATPase.
abstract: We studied, in the rat brain, the synaptosomal and microsomal membrane fractions of Cl⁻ ion-activated, Mg²⁺-dependent ATPase, satisfying the necessary kinetic peculiarities of transport ATPases, by a novel method of kinetic analysis of the multisite enzyme systems: (1) the [Mg-ATP] complex constitutes the substrate of the enzymic reaction; (2) the V = f(Cl⁻) dependence-reflecting curve is bell-shaped; (3) substrate dependence, V = f(S), curves at a constant concentration of free ligands (Mg(f), ATP(f), Cl⁻); (4) as known from the literature, in the process of reaction a phosphorylated intermediate is formed (Gerencser, Crit Rev Biochem Mol Biol 31:303-337, 1996). We report on the Cl-ATPase molecular mechanism and its place in the "P-type ATPase" classification.
authors.affiliation: Beritashvili Institute of Physiology, 14 Gotua str, 0160 Tbilisi, Georgia. dsopio@yahoo.com
authors.forename: Sopio
authors.initials: S
authors.lastname: Dzneladze
authors.forename: Leila
authors.initials: L
authors.lastname: Tsakadze
authors.forename: Marina
authors.initials: M
authors.lastname: Leladze
authors.forename: Zurab
authors.initials: Z
authors.lastname: Kometiani
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D027321:Anion Transport Proteins / Q000378:metabolism*; D001921:Brain / Q000201:enzymology; D002462:Cell Membrane / Q000201:enzymology; D002712:Chlorides / Q000378:metabolism; D006868:Hydrolysis; D007700:Kinetics; D051381:Rats
chemical_list: D027321:Anion Transport Proteins; D002712:Chlorides; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C031652:anion-sensitive ATPases