- Sept. 22, 2020
-- Phenylalanine Ammonia-Lyase (PAL, EC 220.127.116.11) catalyzes the reversible non-oxidative deamination of L-phenylalanine to transcinnamic acid and ammonia without any external cofactors. PAL is expressed in plants, yeast and some fungi and is absent in bacteria and animals. Patients suffering from the genetic disorder, phenylketonuria is unable to metabolize phenylalanine that leads to irreversible cognitive impairment. Historically, phenylketonuria has been treated with a phenylalanine-
restricted diet taken for the entirety of the patient's life. Recently, a drug containing PEGylated PAL has been FDA-approved to treat phenylketonuria, limiting the need of a restricted diet. BioVision's Phenylalanine Ammonia-Lyase Activity Assay Kit measures the activity of PAL via a two-step plate-based assay. The products of the PAL enzymatic reaction, generated in the first step, react with the developers resulting in the formation of a fluorescent compound, which is detected at Ex/Em = 410/470 nm. The kit can detect as low as 3 µU (3 pmol substrate catalysis/minute)
of PAL under assay conditions.
Figures. (a). Ammonium Chloride Standard Curve. (b). Pooled normal human male AB serum was spiked with 5.5, 9.3, 12.7 and 20.6 µU of PAL respectively. The corresponding units of PAL recovered were 4.3, 8.8, 13.2 and 19.7 µU (recovery rates ranging from 78.4- 103.7%). The data shown is the average of three replicates where experiments were performed according to the kit protocol.
For more information on this assay kit, visit:https://bit.ly/3clJWDw