Immunological properties of membrane-bound adenosine triphosphatase. Immunological identification of rutamycin-sensitive F 0·F 1ATPase from Micrococcus luteus atcc 4698 established by crossed immunoelectrophoresis

Abstract

1. (1) F 0·F 1ATPase (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 MgCl 2. 2. (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 F 0·F 1ATPase activity. 3. (3) F 0·F 1ATPase activity is completely inhibited by anti-F 1ATPase antibodies. The inhibition is non-competitive. 4. (4) Crossed immunoelectrophoresis reveals a reaction of immunological identity of F 0·F 1ATPase and F 1ATPase indicating that both enzymes have in common antigenic sites.