Tonoplast ATPase from peanut seedlings
1994
Sen, S. | Sharma, V.
Partially purified tonoplast ATPase from seven-day-old peanut seedlings shows a Km and Vmax 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 400000-600000 with Mr 69000, 55000 and 20000 major polypeptides. A polypeptide of 37000 is also present in minor amounts.
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