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By using an antiserum raised against rat liver tyrosine aminotransferase, it was shown that about 60% of tryptophan aminotransferase activity in rat liver extracts is catalysed by this enzyme. Induction of tryptophan aminotransferase activity by intraperitoneal injections of tryptophan or triamcinolone can be entirely attributed to the effects of these agents on tyrosine aminotransferase. The origin of the other 40% of tryptophan aminotransferase activity remains to be established. This activity increases after starvation for 48 h. It is unlikely that tryptophan transamination plays a quantitatively important role in the metabolism of tryptophan by the liver.
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