Search results for "Oxidative Phosphorylation Coupling Factors"
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Purification, subunit structure, and kinetics of the chloroform-released F1ATPase complex from Rhodospirillum rubrum and its comparison with F1ATPase…
1979
Abstract A stable and homogeneous adenosine-5ʹ-triphosphatase (ATPase, EC 3.6.1.3) has been solubilized from Rhodospirillum rubrum (R . rubrum) chromatophores by chloroform extraction. Purification of the Ca2+-dependent ATPase activity was 200-fold. Ca2+ can be replaced by Mg2+, Cd2+, and Mn2+ .The Km for Ca-ATP (0.17 mᴍ) is increased about 5-fold during solubilization of the enzyme, whereas the Km values for Mg-ATP (0.029 mᴍ) and Cd-ATP (0.014 mᴍ) are not affected. The chloroform-released ATPase has a molecular weight of 400,000 ± 30,000 and consists of the following subunits (molecular weights in parenthesis): α (58,000), β (53,500), γ (39,000), δ (18,500), and ε (14,000). The amino acid …
Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100
1979
1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5…