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Characterization of the membrane-bound ATPase from a facultatively anaerobic alkalophile
1Chemistry Department, College of Arts and Sciences, Chiba University, Japan.
Biochimica Et Biophysica Acta
|April 14, 1989
Abstract:
We have studied the properties of membrane-bound ATPase of a facultatively anaerobic alkalophile. The enzyme could not be solubilized without detergent, suggesting an integral membrane protein. The activity was accelerated by NH4+ and acetate anion, and inhibited by NH3-. The enzyme required Mg2+ or Mn2+ as a divalent cation for the maximal activity. In addition to ATP, the enzyme utilized other triphosphates of nucleosides as a substrate, but not di- nor monophosphates. The enzyme was suggested to crossreact with an antibody against the alpha-subunit of Na+/K+-ATPase from dog kidney.