Vacuolar H+-pyrophosphatase purified from pear fruit

Yasuo Suzuki, Yoshinori Kanayama, Katsuhiro Shiratake, Shohei Yamaki

    Research output: Contribution to journalArticlepeer-review

    20 Citations (Scopus)


    A vacuolar H+ -translocating inorganic pyrophosphatase was purified from pear fruit through selective detergent treatments, Superose 6 and Mono Q column chromatography. The specific activity of the purified enzyme was 850 μmol h-1 mg protein-1. The Mr of V-PPase was 66 kDa by SDS-PAGE and the polypeptide cross-reacted with the antiserum against V-PPase of mung bean. The purified V-PPase was stimulated by potassium and inhibited by calcium and N, N'-dicyclohexylcarbodiimide.

    Original languageEnglish
    Pages (from-to)535-539
    Number of pages5
    Issue number4
    Publication statusPublished - 1999 Feb 24


    • Enzyme purification
    • Pear fruit
    • Pyrus communis
    • Rosaceae
    • Tonoplast
    • Vacuolar H- translocating inorganic pyrophosphatase

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Plant Science
    • Horticulture


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