Abstract
Compounds that activate tryptophan pyrrolase in other animals like methylene blue, hematin, EDTA, and calciumion did not affect fish enzyme activity. Neutralized ascorbic acid showed an inhibitory effect. Time-activity and enzyme concentration-activity curves were determined in three methods of assay. Km was estimated via the Lineweaver-Burk plot to be 80mM. The enzyme was partially purified by a four-step process: solubilization, DEAE Sephadex A-50 chromatography (batch method), and by two consecutive DEAE Sepharose CL-6B chromatographs. The partially purified enzyme was highly unstable so that no characterization was at all possible.
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