Abstract
Peroxidase (EC 1.11.1.7) isozymes from Triticum aestivum L. leaves, showing also phenoloxidase (EC 1.10.3.1; EC 1.10.3.2; EC 1.14.18.1) activity, were partially purified to confirm their polyfunctional nature. After high-resolution anion exchange chromatography, three POD-active peaks were eluted, corresponding to basic-, neutral- and acidic-pI isozymes. The number and mobility of peroxidase isoforms, as well as their ability to act as phenoloxidase, were not modified by the purification procedure. Isozymes possessing only phenoloxidase activity were not found in the purified fractions.
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