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Plant Physiology 84:1402-1407 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Characterization of a Cytosolic Aconitase in Higher Plant Cells

Renaud Brouquisse, Mikio Nishimura1, Jacques Gaillard2 and Roland Douce

Laboratoire de Physiologie Cellulaire Végétale, U.A. CNRS No. 576, DRF, CENG and USMG, 85 X, F-38041 Grenoble-Cédex, France

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.

1 Recipient of an award from the Japan Society for the Promotion of Science and Centre National de la Recherche Scientifique under the Japan-France cooperative Science Programme, 1985. Present address: Nagoya University, Faculty of Agriculture, Chikusa, Nagoya 464, Japan.

2 Present address: DRF/S.Ph-S.C.P.M., CENG, 85X, F-38041 Grenoble-Cedex, France.




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Copyright © 1987 by the American Society of Plant Biologists