Abstract
An improved method of assay is presented for arogenate dehydratase, an enzyme catalyzing the formation of l-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 4, 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 4 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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