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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
Artikel, Bibliographie

Kurzbeschreibung (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.

Typ des Eintrags: Artikel
Erschienen: 1995
Autor(en): Becker, Andrea ; Canut, Herve ; Lüttge, Ulrich ; Maeshima, Masayoshi ; Marigo, Gerard ; Ratajczak, Rafael
Art des Eintrags: Bibliographie
Titel: 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
Sprache: Englisch
Publikationsjahr: 1 Mai 1995
Verlag: Elsevier
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Journal of plant physiology
Jahrgang/Volume einer Zeitschrift: 146
(Heft-)Nummer: 1-2
DOI: 10.1016/S0176-1617(11)81972-3
Kurzbeschreibung (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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Botanischer Garten
Hinterlegungsdatum: 19 Nov 2008 15:57
Letzte Änderung: 11 Aug 2023 14:39
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