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An assay for activity of arogenate dehydratase based upon the selective oxidation of arogenate

✍ Scribed by Charles L. Shapiro; Roy A. Jensen; Karl A. Wilson; John R. Bowen

Publisher: Elsevier Science
Year: 1981
Tongue: English
Weight: 341 KB
Volume: 110
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(81)90106-8

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✦ Synopsis

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 phenylalanine. Following removal of excess KMnO,, the phenylalanine present is measured fluorometrically under optimal conditions. A convenient qualitative test for the completeness of arogenate oxidation in the presence of other molecules which are oxidized by KMnO, is described. A rigorous evaluation of phenylalanine measurement by the method reported here was accomplished by comparison with three other methods, including amino acid analysis.

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