Catalytic properties of the membrane-bound ATPase of anaerobic bacterium Lactobacillus caseiстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 9 декабря 2018 г.
Аннотация:Membrane fragments of Lactobacillus casei possess Mg2+-stimulated DCCD-sensitive ATPase activity (0.3-0.5 (μmol/min per mg of protein) with Km for ATP of about 1 mM. Mg2+-stimulated ATPase activity of membranes is maximal at pH 6.0-6.2 and decreases sharply when pH rises to 6.7. Mg2+-ATPase activity of membranes is stimulated by sulfite and octylglucoside. In the presence of ATP-regenerating system, ATPase activity of membranes decreases in the course of ATP hydrolysis. This decrease is prevented by sulfite. Azide has no effect on the initial rate of ATP hydrolysis but enhances markedly the decrease of enzyme activity during ATP hydrolysis. Half-maximal inhibition of Mg2+-stimulated ATPase activity is caused by 15 μM azide. The inhibitory action of azide is reversed by sulfite. It follows from the results presented that there is an ATPase of FoF1-type in the membranes of L. casei.