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Cellular location of peroxidase isoenzymes in leaf tissue of Petunia and their affinity for Concanavalin A-Sepharose

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Abstract

The cellular location of three peroxidase isoenzymes (PRX) in mature leaf tissue of Petunia and their affinity for Concanavalin A-Sepharose were investigated. The isoenzymes PRXa, PRXb and PRXc were identified by their positions in starch-gel zymograms. The fast-moving anodic and cathodic peroxidase bands, the isoenzymes PRXa and PRXc respectively, were the most active peroxidases in extracellular extracts. The molecular forms of PRXa showed a tissue-specific distribution between midrib and remaining leaf tissue. An intermediate-moving anodic peroxidase band, the isoenzyme PRXb, was the most active peroxidase released after extraction of isolated mesophyll protoplasts. Small amounts of the peroxidase isoenzymes were present in cell-wall-bound fractions. Incubation of a crude protein fraction with Concanavalin A-Sepharose showed that the isoenzyme PRXb bound more firmly to Concanavalin A-Sepharose than the isoenzymes PRXa and PRXc, of which only one molecular form bound partly. The results are discussed with respect to a possible function of one of the peroxidase isoenzymes, and a possible role of oligosaccharide chains in determining the cellular location of plant peroxidases is suggested.

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Abbreviations

Con A:

Concanavalin A

PRX:

peroxidase (isoenzyme)

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Authors and Affiliations

  1. Vakgroep Genetica, Genetisch Institut der Universiteit, Kruislaan 318, NL-1098 SM, Amsterdam, The Netherlands

    Theo Hendriks, Bartel M. van den Berg & André W. Schram

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  1. Theo Hendriks
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  2. Bartel M. van den Berg
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  3. André W. Schram
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Hendriks, T., van den Berg, B.M. & Schram, A.W. Cellular location of peroxidase isoenzymes in leaf tissue of Petunia and their affinity for Concanavalin A-Sepharose. Planta 164, 89–95 (1985). https://doi.org/10.1007/BF00391030

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