An improved method of assay is presented for arogenate dehydratase, an enzyme catalyzing the formation of t.-phenylalanine from L-arogenate. The improvement consists of the inclusion of a step in which arogenate is selectively oxidized using potassium permanganate prior to the measurement of phenyla
A simple spectrophotometric assay for arogenate dehydratase
β Scribed by Suhail Ahmad; Roy A. Jensen
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 404 KB
- Volume
- 163
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A simple spectrophotometric assay for arogenate dehydratase, tile enzyme that catalyzes the formation of L-phenylalanine from L-arogenate, is presented. The method couples the arogenate dehydratase reaction with that of an aromatic aminotransferase partially purified from Acinetobacter calcoaceticus. In the presence of 2-ketoglutarate, phenylpyruvate formation is measured at 320 nm at basic pH. The method was compared with two other methods already in use in our laboratory for arogenate dehydratase. The new method is simple, quick, fairly sensitive, and especially suitable for the screening of a large number of samples. o 1987 Academic FTes, Inc.
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