Abstract
Partially purified tonoplast ATPase from seven-day-old peanut seedlings shows a K m and V m 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 NO 3 −. The enzyme is most effective with Mg 2+ 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 M r 400 000–600 000 with M r 69 000, 55 000 and 20 000 major polypeptides. A polypeptide of 37 000 is also present in minor amounts.
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