Abstract
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 language | English |
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Pages (from-to) | 535-539 |
Number of pages | 5 |
Journal | Phytochemistry |
Volume | 50 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1999 Feb 24 |
Keywords
- Enzyme purification
- Pear fruit
- Pyrus communis
- Rosaceae
- Tonoplast
- Vacuolar H- translocating inorganic pyrophosphatase
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Plant Science
- Horticulture