Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Assay for activity of arogenate dehydratase based upon the selective oxidation of arogenate

Journal Article · · Anal. Biochem.; (United States)
An improved method of assay is presented for arogenate dehydratase, an enzyme catalyzing the formation of L-phenylalamine 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/sub 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/sub 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.
Research Organization:
State Univ. of New York, Binghamton
OSTI ID:
6462856
Journal Information:
Anal. Biochem.; (United States), Journal Name: Anal. Biochem.; (United States) Vol. 110:1; ISSN ANBCA
Country of Publication:
United States
Language:
English