Abstract
Eight constitutive isoperoxidases were separated by the disc method of polyacrylamide gel electrophoresis from a lyophilized extract of 8-day-old oat (Avena sativa L., cv. Victory) coleoptiles. Both anodic and cathodic isoperoxidases were studied and differences in electrophoretic mobilities and hydrogen donor substrate specificities were revealed. In addition, by enzyme assay, cathodic and anodic isoenzymes were shown to possess differences in peroxidase and IAA (indole-3-acetic acid) oxidase activities.Treatment of coleoptiles with 0.07 mM IAA for 24 h resulted in the repression of two slow-migrating anodic isoperoxidases; however, the same treatment also resulted in the induction of two slow-migrating cathodic isoenzymes which were shown to exhibit peroxidase and IAA oxidase activities.
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