Characterization of the membrane-bound ATPase from a facultatively anaerobic alkalophile.
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.
Koyama
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Chemistry Department, College of Arts and Sciences, Chiba University, Japan.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000255:Adenosine Triphosphate; D000643:Ammonium Chloride; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D001665:Binding Sites; D002462:Cell Membrane / Q000201:enzymology*; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D015151:Immunoblotting; D012995:Solubility; D013379:Substrate Specificity
D003902:Detergents; D000643:Ammonium Chloride; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases