[Membrane ATPase of Vibrio alginolyticus. Ion transport activity and homology with F0F1-ATPase from E. coli].
F0F1-ATPase has been isolated from the marine alkali-resistant bacterium Vibrio alginolyticus. The enzyme subunits cross-reacted with antibodies against subunits alpha, beta, gamma, epsilon, and b of E. coli ATPase. The purified ATPase was reconstituted into liposomes effecting an ATP-dependent uptake of H+. Proton transport was inhibited by the ATPase blockers DCCD, triphenyltin, and venturicidin. Na+ ions had no effect on ATP-dependent proton transport. No ATP-dependent transport of Na+ was detected in proteoliposomes.
Dmitriev
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Dann
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Krasnosel'skaia
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Skulachev
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D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001345:Autoradiography; D001692:Biological Transport; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone / Q000737:chemistry; D002412:Cations; D002462:Cell Membrane / Q000201:enzymology; D004229:Dithiothreitol / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000201:enzymology*; D008278:Magnesium Sulfate / Q000737:chemistry; D011510:Proteolipids; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism; D014733:Vibrio / Q000201:enzymology*
D002412:Cations; D011510:Proteolipids; C020485:proteoliposomes; D002259:Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; D008278:Magnesium Sulfate; D012964:Sodium; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; D004229:Dithiothreitol
Membrannaia ATPaza Vibrio alginolyticus. Ion-transportnaia aktivnost' i gomologiia s F0F1-ATPazoĭ E. coli.