Immunological properties of membrane-bound adenosine triphosphatase. Immunological identification of Rutamycin (cas 1404-59-7)-sensitive F0·F1ATPase from Micrococcus luteus atcc 4698 established by crossed immunoelectrophoresis

Add time:09/07/2019    Source:sciencedirect.com

1.(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.(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.(3) F0·F1ATPase activity is completely inhibited by anti-F1ATPase antibodies. The inhibition is non-competitive.4.(4) Crossed immunoelectrophoresis reveals a reaction of immunological identity of F0·F1ATPase and F1ATPase indicating that both enzymes have in common antigenic sites.

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