Characterization of a Cytosolic Aconitase in Higher Plant Cells | Zendy

Renaud Brouquisse | Zendy; Mikio Nishimura | Zendy; Jacques Gaillard | Zendy; Roland Douce | Zendy

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Characterization of a Cytosolic Aconitase in Higher Plant Cells

Author(s) -

Renaud Brouquisse,

Mikio Nishimura,

Jacques Gaillard,

Roland Douce

Publication year - 1987

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.84.4.1402

Subject(s) - aconitase , cytosol , acer pseudoplatanus , fumarase , isozyme , biochemistry , amyloplast , protoplast , chemistry , enzyme , biology , chloroplast , gene , plastid

Protoplasts obtained from sycamore (Acer pseudoplatanus) cell suspensions were found to be highly intact. If the protoplasts were taken up and expelled through a fine nylon mesh, all the protoplasts were ruptured leaving the fragile amyloplasts largely intact. Aconitase hydratase (citrate [isocitrate] hydro-lyase, EC 4.2.1.3) activity of sycamore cells was associated with two protein fractions, one present in the cytosol while the second is of mitochondrial origin. Chromatography on DEAE-trisacryl did not separate the aconitase hydratase isoenzymes. EPR studies established that both isoenzymes exhibited an EPR signal at g = 2.03 once oxidized.

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