Vacuolar H+-pyrophosphatase purified from pear fruit

Yasuo Suzuki; Yoshinori Kanayama; Katsuhiro Shiratake; Shohei Yamaki

doi:10.1016/S0031-9422(98)00554-8

Vacuolar H⁺-pyrophosphatase purified from pear fruit

Yasuo Suzuki, Yoshinori Kanayama, Katsuhiro Shiratake, Shohei Yamaki

AGR - Biological Resource Sciences

Research output: Contribution to journal › Article › peer-review

18 Citations (Scopus)

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
Pages (from-to)	535-539
Number of pages	5
Journal	Phytochemistry
Volume	50
Issue number	4
DOIs	https://doi.org/10.1016/S0031-9422(98)00554-8
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

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title = "Vacuolar H+-pyrophosphatase purified from pear fruit",

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.",

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T1 - Vacuolar H+-pyrophosphatase purified from pear fruit

AU - Suzuki, Yasuo

AU - Kanayama, Yoshinori

AU - Shiratake, Katsuhiro

AU - Yamaki, Shohei

PY - 1999/2/24

Y1 - 1999/2/24

N2 - 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.

AB - 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.

KW - Enzyme purification

KW - Pear fruit

KW - Pyrus communis

KW - Rosaceae

KW - Tonoplast

KW - Vacuolar H- translocating inorganic pyrophosphatase

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