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Subcellular localization of 1-aminocyclopropane-1-carboxylate oxidase in tomato cells

Dieter Reinhardt, Hans Kende and Thomas Boller
Planta
Vol. 195, No. 1 (1994), pp. 142-146
Published by: Springer
Stable URL: http://www.jstor.org/stable/23383080
Page Count: 5
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Subcellular localization of 1-aminocyclopropane-1-carboxylate oxidase in tomato cells
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Abstract

The localization of 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase was examined in suspension-cultured cells of tomato (Lycopersicon esculentum Mill.), using cell-fractionation techniques, followed by immunoblot analysis with monospecific antibodies raised against a tomato ACC oxidase expressed in Escherichia coli. When assayed in vivo, ACC oxidase had a low activity in untreated tomato cells but was strongly induced when the cells were supplied with its substrate, ACC. Immunoblots showed that this induction was accompanied by the accumulation of a single protein corresponding to ACC oxidase, with an apparent molecular mass (Mr) of 36 kDa. The level of this protein in induced cells, estimated by immunoblotting, was compared with that in protoplasts and vacuoles, and with that in various particulate and soluble fractions obtained by differential centrifugation of cell homogenates. It was found that the ACC oxidase antigen was absent from the vacuole, and that most of it was localized in the cytoplasm of the protoplasts without being associated with membranes. Measurements of ACC oxidase activity in preparations of protoplasts and vacuoles supported these results.

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