Immunological and reconstitution studies on the adenosine triphosphatase complex from Rhodospirillum rubrum |
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Authors: | Hans Werner Müller Manfred Schmitt Erwin Schneider Klaus Dose |
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Institution: | Institut für Biochemie, Johannes Gutenberg-Universität, J.J. Becher-Weg 30, D-6500 Mainz F.R.G. |
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Abstract: | Studies on restoration of membrane-bound adenosinetriphosphatase (ATP phosphohydrolase, EC 3.6.1.3) from Rhodospirillum rubrum show that the δ-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. |
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Keywords: | ATPase complex Reconstitution (Rhodospirillum rubrum) |
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