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- W2922271792 endingPage "958" @default.
- W2922271792 startingPage "958" @default.
- W2922271792 abstract "The plasma membrane H+-ATPase was purified from the yeast K. lactis. The oligomeric state of the H+-ATPase is not known. Size exclusion chromatography displayed two macromolecular assembly states (MASs) of different sizes for the solubilized enzyme. Blue native electrophoresis (BN-PAGE) showed the H+-ATPase hexamer in both MASs as the sole/main oligomeric state—in the aggregated and free state. The hexameric state was confirmed in dodecyl maltoside-treated plasma membranes by Western-Blot. Tetramers, dimers, and monomers were present in negligible amounts, thus depicting the oligomerization pathway with the dimer as the oligomerization unit. H+-ATPase kinetics was cooperative (n~1.9), and importantly, in both MASs significant differences were determined in intrinsic fluorescence intensity, nucleotide affinity and Vmax; hence suggesting the large MAS as the activated state of the H+-ATPase. It is concluded that the quaternary structure of the H+-ATPase is the hexamer and that a relationship seems to exist between ATPase function and the aggregation state of the hexamer." @default.
- W2922271792 created "2019-03-22" @default.
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- W2922271792 date "2019-03-08" @default.
- W2922271792 modified "2023-10-01" @default.
- W2922271792 title "The Oligomeric State of the Plasma Membrane H+-ATPase from Kluyveromyces lactis" @default.
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- W2922271792 doi "https://doi.org/10.3390/molecules24050958" @default.
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