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Part of the book series: Advances in Agricultural Biotechnology ((AABI,volume 26))

Abstract

Previous work showed that activity of the EFE almost completely disappears when plant tissues are converted to isolated cells and protoplasts by the action of cell-wall degrading enzymes. The results presented in the present paper show that EFE activity is largely retained when slices of apple (Malus sylvestris) tissue are incubated in the presence of the cell-wall degrading enzymes, Pectolyase and Caylase, even though the action of these enzymes results in the loss of cell wall material so that >90% of the tissue can pass through a 0.2 mm mesh. Activity of the EFE disappears after this treatment only when the cells and protoplasts are released from the tissue.

Membranes present in the juice squeezed from ripe kiwifruit (Actinidia deliciosa) possess an EFE activity which shows the two essential features of the enzyme activity observed in vivo: a preference for the racemic mixture containing the (1R, 2S)-enantiomer of 1-amino-2-ethylcyclopropane-1-carboxylic acid, and a relatively high affinity for ACC (apparent Km of 0.125 mM). In addition, the EFE activity of the kiwifruit membranes resembles the in vivo activity in its requirement for membrane integrity, as revealed by the loss of activity when the membrane vesicles are denied osmotic support. Fractionation of these membranes on continuous density gradients reveals that the EFE activity is confined to a particular species of membrane vesicle. Marker enzymes have been assayed to indicate the nature of the EFE-bearing membranes.

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© 1989 Kluwer Academic Publishers

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John, P., Mitchell, T., Razdan, A., Ververidis, P. (1989). Characterization of the Ethylene-Forming Enzyme in Vivo and in Vitro . In: Clijsters, H., De Proft, M., Marcelle, R., Van Poucke, M. (eds) Biochemical and Physiological Aspects of Ethylene Production in Lower and Higher Plants. Advances in Agricultural Biotechnology, vol 26. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-1271-7_3

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  • DOI: https://doi.org/10.1007/978-94-009-1271-7_3

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-7065-2

  • Online ISBN: 978-94-009-1271-7

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