Abstract
A possible error in spectrophotometric determination of cinnamate, the product of phenylalanine ammonia-lyase activity, using nonpurified protein extracts has been shown.
Under optimal conditions for phenylalanine ammonia-lyase activity, with borate buffer and in the presence of α-keto acids, phenylpyruvate is produced and its enol tautomer-borate complex formed, strongly absorbs at 290 nanometers.
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