Vacuolar H+-pyrophosphatase purified from pear fruit

Yasuo Suzuki, Yoshinori Kanayama, Katsuhiro Shiratake, Shohei Yamaki

Research output: Contribution to journalArticlepeer-review

18 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


Dive into the research topics of 'Vacuolar H<sup>+</sup>-pyrophosphatase purified from pear fruit'. Together they form a unique fingerprint.

Cite this