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    Expression of horseradish peroxidase in transgenic tobacco


    Pellegrineschi, A. and Kist, M. and Dix, Ilona and Kavanagh, T.A. and Dix, Philip (1995) Expression of horseradish peroxidase in transgenic tobacco. Biochemical Society Transactions, 23 (2). pp. 247-250. ISSN 0300-5127

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    Abstract

    Peroxidases are common oxidoreductases present in plants, animals and micro-organisms. Plant peroxidases are classified as basic, neutral or acidic enzymes, depending on their profiles of elution during ion-exchange column chromatography or isoelectric points [ 11. Horseradish (Amtoru~hru sticuna) peroxidases (HRPs; EC 1.1 1.1.7), are probably the best characterized of these enzymes. They are believed to be involved in plant responses to a number of biotic and abiotic stresses, notably in the disruption of free radicals and active derivatives of oxygen. The effects of these molecules have been well described [2], and in general the presence of these compounds are ‘highly destructive’ for cell metabolism. However, these oxygen derivatives are involved in halogenation and hydroxylation reactions in peroxisomes and in the cell wall, suggesting that the plant cell needs a fine regulation between production and destruction of oxygen radicals. A key to the comprehension of the role of peroxidase activity in this and other stress responses could be the study of the effect of modified expression and targeting of peroxidase activity in transgenic plants. The present report describes the production of such tobacco plants using a synthetic HRP gene [ 31, with a range of regulatory and targeting sequences.

    Item Type: Article
    Keywords: Expression; horseradish peroxidase; transgenic tobacco; oxidoreductases;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 7387
    Identification Number: https://doi.org/10.1042/bst0230247
    Depositing User: Prof. Philip J. Dix
    Date Deposited: 26 Aug 2016 10:43
    Journal or Publication Title: Biochemical Society Transactions
    Publisher: Portland Press
    Refereed: No
    URI:

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