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Research ArticleMetabolism and Enzymology
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Characterization of a Cytosolic Aconitase in Higher Plant Cells

Renaud Brouquisse, Mikio Nishimura, Jacques Gaillard, Roland Douce
Renaud Brouquisse
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Mikio Nishimura
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Jacques Gaillard
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Roland Douce
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Published August 1987. DOI: https://doi.org/10.1104/pp.84.4.1402

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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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Characterization of a Cytosolic Aconitase in Higher Plant Cells
Renaud Brouquisse, Mikio Nishimura, Jacques Gaillard, Roland Douce
Plant Physiology Aug 1987, 84 (4) 1402-1407; DOI: 10.1104/pp.84.4.1402

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Characterization of a Cytosolic Aconitase in Higher Plant Cells
Renaud Brouquisse, Mikio Nishimura, Jacques Gaillard, Roland Douce
Plant Physiology Aug 1987, 84 (4) 1402-1407; DOI: 10.1104/pp.84.4.1402
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Plant Physiology
Vol. 84, Issue 4
August 1987
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More in this TOC Section

  • Distribution of Pyruvate Dehydrogenase Complex Activities between Chloroplasts and Mitochondria from Leaves of Different Species
  • Identification of Posttranslationally Modified 18-Kilodalton Protein from Rice as Eukaryotic Translation Initiation Factor 5A
  • Regulation of Maize Leaf Nitrate Reductase Activity Involves Both Gene Expression and Protein Phosphorylation
Show more Metabolism and Enzymology

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