The oxidation of tryptophan in pea-seedling tissues and extracts

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Abstract
The oxidation of tryptophan by pea-seedling tissue slices and extracts was accelerated by putrescine and ethanol-amine. The product showed new absorption maxima at 270 and 370 mil. Purification of the enzyme was accomplished by centrifugation and precipitation of protein with immiscible solvents. Isoelectric precipitation and absorption on Ca phosphate gel separated amine-oxidase and peroxidase activity, with the tryptophan-oxidizing activity associated with the latter. In purified extracts, 2 molecules of H2O2 oxidized one molecule of tryptophan giving a reddish-brown product. Tryptophan was oxidized by purified horseradish peroxidase with -free H2O2 or with peroxide-forming enzymes and substrates.