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- W2069125844 abstract "Abstract Partially purified tonoplast ATPase from seven-day-old peanut seedlings shows a Km and Vm value of 0.15 mM and 0.86 nkat Pi mg−1 protein, respectively. The enzyme is stimulated by Cl− and monovalent cations and inhibited by NO3−. The enzyme is most effective with Mg2+ ATP as the substrate. The purified enzyme is highly unstable and requires phospholipids for activity. SDS-PAGE analysis of tonoplast ATPase shows it to be a multimeric structure of Mr 400 000–600 000 with Mr 69 000, 55 000 and 20 000 major polypeptides. A polypeptide of 37 000 is also present in minor amounts." @default.
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- W2069125844 date "1994-06-01" @default.
- W2069125844 modified "2023-09-26" @default.
- W2069125844 title "Tonoplast ATPase from peanut seedlings" @default.
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- W2069125844 doi "https://doi.org/10.1016/s0031-9422(00)89776-9" @default.
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