Immunological properties of membrane-bound adenosine triphosphatase: immunological identification of rutamycin-sensitive F0.F1ATPase from Micrococcus luteus ATCC 4698 established by crossed immunoelectrophoresis.
(1) F0.F1ATPase (EC 3.6.1.3) from Micrococcus luteus ATCC 4698 was solubilized from plasma membranes by the non-ionic detergent Triton X-100 in the presence of 0.05 M MgCl2. (2) The antibiotics rutamycin, Dio-9, quercetin, oligomycin, botrycidin, efrapeptin, leucinostatin, valinomycin, and venturicidin as well as N,N'-dicyclohexylcarbodiimide and dinitrophenol are potent inhibitors of F0.F1ATPase activity.(3) F0.F1ATPase activity is completely inhibited by anti-F1ATPase antibodies. The inhibition is non-competitive. (4) Crossed immunoelectrophoresis reveals a reaction of immunological identity of F0.F1ATPase and F1ATPase indicating that both enzymes have in common antigenic sites.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000276:immunology* / Q000302:isolation & purification; D000935:Antifungal Agents / Q000494:pharmacology*; D002462:Cell Membrane / Q000201:enzymology; D000939:Epitopes; D007123:Immunoelectrophoresis, Two-Dimensional; D008837:Micrococcus / Q000201:enzymology; D008968:Molecular Conformation; D012427:Rutamycin / Q000494:pharmacology*
D000935:Antifungal Agents; D000939:Epitopes; D012427:Rutamycin; D000251:Adenosine Triphosphatases