title: Mn2+-stimulated ATPase in rat brain.
abstract: Divalent cation ATPases were prepared from rat brain synaptic vesicles, synaptosomal plasma membranes, and plasma membranes from the brain stem and sciatic nerve and tested for optimal stimulation by Mn2+, Mg2+, or Ca2+. ATPase in the synaptic vesicle subfraction was optimally stimulated by Mn2+. All plasma membrane preparations were optimally stimulated by Mg2+. Separate Mn2+ and Mg2+ ATPases could not be distinguished by either chemical inactivation or substrate preference criteria. Mn2+ stimulated ATPase in the micromolar range and it is suggested that Mn2+ interaction with ATPase may be of physiological and/or toxicological importance by being related to the cellular metabolism of this element.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002413:Cations, Divalent; D002462:Cell Membrane / Q000201:enzymology; D007700:Kinetics; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012584:Sciatic Nerve / Q000201:enzymology; D013572:Synaptic Vesicles / Q000201:enzymology*; D013574:Synaptosomes / Q000201:enzymology
chemical_list: D002413:Cations, Divalent; D000251:Adenosine Triphosphatases; C032304:manganese ATPase