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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
