[Nature of membrane ATPase inactivation in an Escherichia coli mutant with genetically impaired ATPase].
Homogeneous preparations of F1 possessing identical subunit composition have been isolated from the mutant strain of E. coli AN 120 with genetically impaired membrane ATPase and from the wild strain of AN 180. Using ion-exchange chromatography, the subunits alpha and beta of F1 were isolated. It was shown that the alpha- and beta-subunits of both active and genetically impaired F1 have similar molecular weights and total electrical charges.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors* / Q000235:genetics / Q000502:physiology*; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009154:Mutation; D006180:Proton-Translocating ATPases; D013045:Species Specificity
D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases
Issledovanie prirody inaktivatsii membrannoi ATPazy u mutanta Escherichia coli s Geneticheskoĭ povrezhdennoĭ ATPazoĭ.