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- W1988472912 abstract "Abstract ATPase was solubilized with n-octylglucoside from plasma membrane-enriched fractions of mature cucumber roots. Partially purified ATPase was prepared by the centrifugation of an n-octylglucoside solubilized sample and reconstituted into proteoliposomes by the n-octylglucoside dilution method. Equilibrium density centrifugation showed that the densities of ATPase reconstituted into proteoliposomes and of ATPase from the native plasma membrane-enriched fraction detected by ATPase activity were 1.115 and 1.175 g cm−3, respectively. The ATPase reconstituted into proteoliposomes showed a high specificity for ATP as a substrate, while other nucleotides, pyrophosphate and p-nitrophenyl-phosphate were hardly hydrolyzed. The optimum pH of the reconstituted ATPase was 6.0 and the K m value for ATP was 0.23 mol m−3. The reconstituted ATPase was inhibited strongly by vanadate and DCCD but not by nitrate. The reconstituted ATPase was activated by various monovalent cations accompanying chloride anion but not ..." @default.
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- W1988472912 date "1993-09-01" @default.
- W1988472912 modified "2023-09-24" @default.
- W1988472912 title "Reconstitution of plasma membrane ATpase from mature cucumber roots" @default.
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- W1988472912 doi "https://doi.org/10.1080/00380768.1993.10419795" @default.
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