Activity and partial purification of liver pyrrolase in rainbow trout
1994
Serrano, A.E. Jr. | Nagayama, F. (Philippines Univ. in the Visayas, Leganes, Iloilo (Philippines). Coll. of Fisheries)
Compounds that activate tryptophan pyrrolase in other animals, such as 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 essay. Kin was estimated via Lineweauer-Brok plot to be 80 mm. The enzyme was partially purified by a four-step process: solubilization, DEAE, Sepharose, and CL-6B chromatographs. The partially purified enzyme was highly unstable, so that no characterization was at all possible
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