Open AccessCharacterization 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.