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ARTICLES
Active phosphorylase was determined in rat livers during the end of the fetal period and the first days of life. This enzyme increases between the 16th day of gestation and birth. After birth, another increase in observed that takes place with 6 h. In the neonatal liver, the rapid increase in active phosphorylase, is inhibited by high levels of blood glucose, but is unaffected by actinomycin D. In fetal liver glucagon administration is followed after 5 h by an increase in total phosphorylase with only a small increase in active phosphorylase; this effect is blocked by actinomycin D. The fetal changes are interpreted as de novo synthesis, whereas the neonatal increase is due to an activation of inactive phosphorylase. Both enzymatic changes appear to be regulated by glycogen. The role of phosphorylase in the regulation of glycogen metabolism in neonatal liver is discussed.
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