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- W2078498052 abstract "Abstract The hydrolytic subunit of the H + -translocating inorganic pyrophosphatase (V-PPase EC 3.6.1.1) prepared from Rubus hispidus cell cultures has been purified from tonoplast-enriched membranes and analysed by SDS-polyacrylamide gel electrophoresis. Only one polypeptide of M r 70 000 was recovered with the V-PPase activity after solubilization in the presence of Triton X-100, purification by gel filtration (Superose) and anion exchange (Mono Q) chromatography. This polypeptide strongly cross-reacted with an antibody raised against the V-PPase from Vigna radiata . The tonoplast-enriched fraction was also used to solubilize and reconstitute the V-PPase. The proteoliposomes showing a PP 1 -dependent proton transport activity were purified by gel filtration (Superose) and analysed by SDS-polyacrylamide gel electrophoresis. Only one polypeptide of M r 70 000 was recovered with the proton-pumping activity. All these data suggest that the native V-PPase from Rubus is composed of a single kind of polypeptide with an M r of 70 000 and representing the catalytic subunit." @default.
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- W2078498052 date "1994-01-01" @default.
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- W2078498052 title "Purification and functional reconstitution of the tonoplast pyrophosphate-dependent proton pump from Rubus hispidus cell cultures" @default.
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- W2078498052 doi "https://doi.org/10.1016/0168-9452(94)03983-6" @default.
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