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Phenylalanine and tyrosine ammonia-lyase activity in Sporobolomyces pararoseus
Authors:J R Parkhurst and D S Hodgins
Institution:

Department of Biochemistry and Molecular Biology, University of Oklahoma School of Medicine, and The Oklahoma Medical Research Foundation, 800 NE 13th Street, Oklahoma City, Oklahoma 73104, U.S.A.

Abstract:Phenylalanine ammonia-lyase from Sporobolomyces pararoseus was purified more than 450-fold. Polyacrylamide disc gel electrophoresis of this purified enzyme gave a single major protein band. Tyrosine ammonia-lyase activity was monitored during the purification of phenylalanine ammonia-lyase. Deaminating activities for phenylalanine and tyrosine were not separated during the purification process. The existence of one ammonia-lyase with bisubstrate activity is postulated.
Keywords:
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