ATPase in isolated membranes of Bacillus subtilis

摘要: Abstract Cytoplasmic membranes from Bacillus subtilis ATCC 6633 were prepared by osmotic shock of protoplasts formed the action lysozyme. The resulting membrane ghosts found to possess both Mg 2+ - and Ca -dependent ATP phosphohydrolase (ATPase, EC 3.6.1.3) activities. A maximal activity 1.67 μmoles orthophosphate released/min per mg protein was obtained at pH 8.7 with -ATPase. Maximal observed a molar ration 0.5 ratio 0.7 7.8. Addition together assay resulted in an inhibition Concentrations excess 2.5 mM inhibited enzyme activities, whereas non-enzymatic hydrolysis concentrations 5 mM. 5′-triphosphates guanosine uridine also hydrolyzed preparations. Na + K each stimulated -ATPase activity. Ouabain did not reverse or -, (Na )-mediated stimulations. influences various metabolic inhibitors other substances on ATPase studied.