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• W2092226866 abstract "Abstract The ATP synthase was isolated from the cytoplasmic membrane of the anaerobic bacterium Wolinella (formerly Vibrio ) succinogenes , using a non-ionic detergent. After 20-fold purification the enzyme was homogeneous. The M r was determined to be 410 000. Gel electrophoresis in the presence of dodecylsulfate separated eight different peptides, seven of which appeared to be subunits of the enzyme ( M r 56 000, 50 000, 36 000, 19 000, 13 000, 11 000 and 8000). Dicyclohexylcarbodiimide (0.6 mol per mol enzyme) was specifically bound to the M r 8000 subunit. In electron micrographs, after negative staining, the enzyme appeared as a dumb-bell having a globular portion of 10.0–10.8 nm diameter on one end. The K i for ADP as a competitive inhibitor of ATP hydrolysis was about 10-times smaller than the K M for ATP. Incorporation of the enzyme into liposomes caused the K i and K M to decrease to values that approached those measured with the bacterial membrane. Treatment of the membrane with CHCl 3 was the only procedure found that could split the ATPase from the ATP synthase. The soluble enzyme isolated after this treatment exhibited a 15-times greater specific activity of ATP hydrolysis than ATP synthase. The ATPase was made up of three different subunits ( M r 56 000, 50 000 and 36 000). The M r was determined to be 340 000. In electron micrographs, after negative staining, the ATPase appeared as spherical particles which were similar to the globular part of the ATP synthase. The particles showed a hexagonal fine structure with a seventh element in the centre of the hexagon, suggesting an α 3 β 3 ρ composition of the enzyme." @default.
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• W2092226866 date "1985-10-01" @default.
• W2092226866 modified "2023-09-27" @default.
• W2092226866 title "Structural and ATP-hydrolyzing properties of the ATP synthase isolated from Wolinella succinogenes" @default.
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• W2092226866 doi "https://doi.org/10.1016/0005-2728(85)90208-7" @default.
• W2092226866 hasPublicationYear "1985" @default.
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