NIPPON SUISAN GAKKAISHI
Online ISSN : 1349-998X
Print ISSN : 0021-5392
ISSN-L : 0021-5392
Activity and Partial Purification of Liver Tryptophan Pyrrolase in Rainbow Trout
Augusto E. SerranoFumio Nagayama
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JOURNAL FREE ACCESS

1992 Volume 58 Issue 12 Pages 2367-2371

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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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© The Japanese Society of Fisheries Science
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