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Purification and immunological comparison of the tonoplast H+-pyrophosphatase from cells of Catharanthus roseus and leaves from Mesembryanthemum crystallinum performing C3-photosynthesis and the obligate CAM plant Kalanchoe daigremontiana

Becker, Andrea ; Canut, Herve ; Lüttge, Ulrich ; Maeshima, Masayoshi ; Marigo, Gerard ; Ratajczak, Rafael (1995)
Purification and immunological comparison of the tonoplast H+-pyrophosphatase from cells of Catharanthus roseus and leaves from Mesembryanthemum crystallinum performing C3-photosynthesis and the obligate CAM plant Kalanchoe daigremontiana.
In: Journal of plant physiology, 146 (1-2)
doi: 10.1016/S0176-1617(11)81972-3
Article, Bibliographie

Abstract

The tonoplast H+-pyrophosphatase (EC 3.6.1.1) from photosynthetically inactive cell cultures of the C3-plant Catharanthus roseus (L.) G. Don., and from leaves of the C3/CAM-intermediate plant Mesembryanthemum crystallinum L. in the C3-state and of the obligate CAM-plant Kalanchoë daigremontiana Hamet et Perrier de la Bâthie, was purified using Mono Q anion-exchange and Superose 6 size-exclusion fast protein liquid chromatography. The combination of both chromatographical techniques led to a single polypeptide with an apparent molecular mass of 72 kDa exhibiting K+-stimulated pyrophosphate hydrolysis activity in preparations from C. roseus and M. crystallinum and to two polypeptides (72 and 70 kDa) in hydrolytic active fractions from K. daigremontiana. These polypeptides cross-reacted with an antiserum against the tonoplast inorganic H+-pyrophosphatase of Vigna radiata L. cv. Wilczek. The possible identity of the 70 kDa polypeptide of K. daigremontiana is discussed.

Item Type: Article
Erschienen: 1995
Creators: Becker, Andrea ; Canut, Herve ; Lüttge, Ulrich ; Maeshima, Masayoshi ; Marigo, Gerard ; Ratajczak, Rafael
Type of entry: Bibliographie
Title: Purification and immunological comparison of the tonoplast H+-pyrophosphatase from cells of Catharanthus roseus and leaves from Mesembryanthemum crystallinum performing C3-photosynthesis and the obligate CAM plant Kalanchoe daigremontiana
Language: English
Date: 1 May 1995
Publisher: Elsevier
Journal or Publication Title: Journal of plant physiology
Volume of the journal: 146
Issue Number: 1-2
DOI: 10.1016/S0176-1617(11)81972-3
Abstract:

The tonoplast H+-pyrophosphatase (EC 3.6.1.1) from photosynthetically inactive cell cultures of the C3-plant Catharanthus roseus (L.) G. Don., and from leaves of the C3/CAM-intermediate plant Mesembryanthemum crystallinum L. in the C3-state and of the obligate CAM-plant Kalanchoë daigremontiana Hamet et Perrier de la Bâthie, was purified using Mono Q anion-exchange and Superose 6 size-exclusion fast protein liquid chromatography. The combination of both chromatographical techniques led to a single polypeptide with an apparent molecular mass of 72 kDa exhibiting K+-stimulated pyrophosphate hydrolysis activity in preparations from C. roseus and M. crystallinum and to two polypeptides (72 and 70 kDa) in hydrolytic active fractions from K. daigremontiana. These polypeptides cross-reacted with an antiserum against the tonoplast inorganic H+-pyrophosphatase of Vigna radiata L. cv. Wilczek. The possible identity of the 70 kDa polypeptide of K. daigremontiana is discussed.

Divisions: 10 Department of Biology
10 Department of Biology > Botanischer Garten
Date Deposited: 19 Nov 2008 15:57
Last Modified: 11 Aug 2023 14:39
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