Abstract
Tryptophan was rapidly destroyed aerobically in the presence of Mn 2+ and sulfite. The rate of destruction was greatly increased when horseradish peroxidase was added. The optimal pH for the reaction was 8.0. The destruction of tryptophan was dependent on the aerobic oxidation of sulfite. Superoxide dismutase inhibited sulfite oxidation and thus inhibited the tryptophan destruction. Tracer studies indicate that tryptophan is converted into at least 4 products.
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