Immunological and reconstitution studies on the adenosine triphosphatase complex from Rhodospirillum rubrum.
Studies on restoration of membrane-bound adenosinetriphosphatase (ATP phosphohydrolase, EC 3.6.1.3) from Rhodospirillum rubrum show that the delta-subunit is capable of binding to the F1 factor or to the F0 moiety of the F0-F1 ATPase complex. This subunit is thus likely involved in linking the F0 and F1 factor. During solubilization of the oligomycin-sensitive F0-F1 ATPase complex with Triton X-100 the detergent becomes specifically associated with the lipophilic F0 part of the enzyme complex. Crossed immunoelectrophoresis, agglutination tests, and kinetic studies with anti-F1 ATPase antibodies reveal a reaction of immunological identity of membrane-bound ATPase, F0-F1 ATPase, and F1 ATPase.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000372:Agglutination Tests; D020130:Bacterial Chromatophores / Q000201:enzymology; D007123:Immunoelectrophoresis, Two-Dimensional; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D009840:Oligomycins / Q000494:pharmacology; D011092:Polyethylene Glycols; D012247:Rhodospirillum rubrum / Q000201:enzymology*; D012995:Solubility
D009840:Oligomycins; D011092:Polyethylene Glycols; D000251:Adenosine Triphosphatases; D008274:Magnesium