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. 1987 Aug;84(4):1402–1407. doi: 10.1104/pp.84.4.1402

Characterization of a Cytosolic Aconitase in Higher Plant Cells

Renaud Brouquisse 1, Mikio Nishimura 1,1, Jacques Gaillard 1,2, Roland Douce 1
PMCID: PMC1056786  PMID: 16665617

Abstract

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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Selected References

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