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- W1567658405 abstract "Abstract The disintegration of Halobacterium cutirubrum cell envelope vesicles at lowered salt concentrations has been followed by electron microscopy, light scattering, and the sedimentation properties of total protein, phospholipids, flavoproteins, and cytochromes. As NaCl concentration is lowered these components are released from the membranes in roughly sequential fashion. Thus, flavoproteins are solubilized at 1.0 to 2.2 m NaCl, the outer envelope at 0.7 to 0.9 m NaCl, cytochrome b and phospholipids at 0 to 1.2 m NaCl, and cytochrome oxidase at 0 to 0.5 m NaCl. Comparison of the effects of NaCl, NaNO3, and NaClO4 revealed that those components which require more than 0.6 to 0.7 m NaCl for stabilization in the membrane exhibited marked specificity among these salts, the order of preference being NaCl g NaNO3 g NaClO4, whereas those components which were stabilized at lower NaCl concentrations showed little salt specificity. The correlation of the effectiveness of these salts in maintaining the integrity of the membrane with salting out character indicates that the binding of the former components is predominantly hydrophobic, while the binding of the latter components is primarily ionic. Evidence consistent with this pattern of binding forces was obtained from the solubilization of membrane proteins with hydrophobic bond-breaking agents." @default.
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- W1567658405 date "1971-07-01" @default.
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- W1567658405 title "Studies of the Electron Transport Chain of Extremely Halophilic Bacteria" @default.
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