1992 Volume 58 Issue 12 Pages 2367-2371
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.