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 NH 4 + and acetate anion, and inhibited by NO 3 −. The enzyme required Mg 2+ or Mn 2+ 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 α-subunit of Na +/K +-ATPase from dog kidney.
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