| Literature DB >> 6600779 |
S J Beevers, R G Knowles, C I Pogson.
Abstract
We describe here a simple and convenient method for assay of tryptophan 5-monooxygenase (hydroxylase), applicable to enzyme in all states of purification. It is based on the enzyme-catalysed formation of 5-hydroxy-[4-3H]tryptophan from [5-3H]tryptophan, and the subsequent acid-dependent quantitative release of 3H as 3H2O; unreacted substrate is removed with activated charcoal. The assay is linear with respect to both protein concentration and time, and gives results similar to those in a standard fluorimetric assay.Entities:
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Year: 1983 PMID: 6600779 DOI: 10.1111/j.1471-4159.1983.tb08066.x
Source DB: PubMed Journal: J Neurochem ISSN: 0022-3042 Impact factor: 5.372