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

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

20 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

Access to Document

10.1016/S0031-9422(98)00554-8

Cite this

@article{08135e78bff9491f9db500402ef0ded4,

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.",

keywords = "Enzyme purification, Pear fruit, Pyrus communis, Rosaceae, Tonoplast, Vacuolar H- translocating inorganic pyrophosphatase",

author = "Yasuo Suzuki and Yoshinori Kanayama and Katsuhiro Shiratake and Shohei Yamaki",

year = "1999",

month = feb,

day = "24",

doi = "10.1016/S0031-9422(98)00554-8",

language = "English",

volume = "50",

pages = "535--539",

journal = "Phytochemistry",

issn = "0031-9422",

publisher = "Elsevier Limited",

number = "4",

}

TY - JOUR

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

UR - http://www.scopus.com/inward/record.url?scp=0033082035&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033082035&partnerID=8YFLogxK

U2 - 10.1016/S0031-9422(98)00554-8

DO - 10.1016/S0031-9422(98)00554-8

M3 - Article

C2 - 10028695

AN - SCOPUS:0033082035

VL - 50

SP - 535

EP - 539

JO - Phytochemistry

JF - Phytochemistry

SN - 0031-9422

IS - 4

ER -