Abstract
The developmental pattern of phenylalanine hydroxylase was studied in rat kidney and compared with that of liver from the same animal. Traces of activity were observed from 19 to 21 days of gestation in the liver and on Day 20 and 21 of gestation in the kidney. Significant amounts of activity were noticed on Day 22 of gestation. Kidney on Day 21 of gestation showed slightly higher values than that seen in corresponding liver. Fetal liver and kidney showed about 30% and 90% activity of newborn animals, respectively. Both synthetic cofactor and organic reductant were necessary for optimal activity of liver and kidney enzymes. pH studies showed an optimum at pH 7.0 in both liver and kidney. Storage at −15 °C resulted in loss of activity in both liver and kidney to the same extent at a given time. No evidence of inhibition of either liver or kidney enzyme by phenylalanine was noticed up to a concentration of 4 μmoles per assay. Heat denaturation studies at 50 °C showed the kidney enzyme to be slightly less stable than the liver enzyme though a similar pattern was observed in both tissues at all ages studied.
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