title: Energy-linked and energy-independent transhydrogenase activities in Escherichia coli vesicles.
abstract: Active transport vesicles of Escherichia coli were shown to possess low levels of energy-independent and energy-dependent nicotinamide nucleotide transhydrogenase activities. Breakage of such vesicles in a French pressure cell resulted in a fraction which had an 8-10-fold increased respiration- and ATP-driven transhydrogenase activities. Stimulation of the ATPase activity in vesicles with Triton X-100 was also paralledled by a 2-fold increase in the energy-independent transhydrogenase. Disruption of the vesicles similarly resulted in increases in the energy-independent transhydrogenase, NADH and succinate oxidase activities but a decrease in succinate supported proline uptake. In the light of these findings, the "sidedness' of the vesicle membranes is discussed.
mesh_terms: D000251:Adenosine Triphosphatases / Q000276:immunology / Q000378:metabolism; D000937:Antigen-Antibody Reactions; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000201:enzymology; D004579:Electron Transport; D004735:Energy Transfer; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D008566:Membranes / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011092:Polyethylene Glycols / Q000494:pharmacology; D013385:Succinate Dehydrogenase / Q000378:metabolism; D013386:Succinates / Q000378:metabolism
chemical_list: D013386:Succinates; D009243:NAD; D011092:Polyethylene Glycols; D013385:Succinate Dehydrogenase; D009247:NADH, NADPH Oxidoreductases; D000251:Adenosine Triphosphatases