Indexed on: 01 Nov '80Published on: 01 Nov '80Published in: Biologia Plantarum
The investigation of the substrate specificity of the anionic peroxidase isoenzymes, isolated from the zone of differentiation of the primary roots ofZea mays, for some representatives of phenolic compounds and aromatic amines, as hydrogen donors, is reported. The investigation was carried out electrophoretically with peroxidase isoenzymes partially purified by a combination of gel filtration by Sephadex G-25 and Sephadex G-100. A difference in the substrate specificity of the individual isoenzymes is observed. It was established that the anionic peroxidase isoenzymes showed a similarity in total number and relative activity on staining with bivalent phenols and difference on staining with trivalent phenols, as hydrogen donors. A greater number of isoenzymes was stained with benzidine ando-dianisidine and a lesser number witho- andp-phenylendiamine. The substrate specificity of the peroxidase isoenzymes was compared for guaiacol and benzidine. The substrate specificity of peroxidase soenzymes was discussed as regards their diverse role in the plant metabolism.