Studies on the Molecular Basis of Development of Serine Dehydratase in Rat Liver

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Abstract
L-Serine dehydratase [EC 4. 2. 1. 18] activity in the liver of newborn rats developed immediately after birth. Pluse-labeling with 14C-amino acids followed by specific precipitation of the enzyme with antiserum showed that the increase in the enzyme activity was due to net synthesis of enzyme protein. Serine dehydratase activity in prenatal liver was low and did not change within 8 hr on exposure of the fetus to the external environment by Caesarean operation after 21 days of gestation, while it increased when glucagon was administered in-traperitoneally to the fetus. Induction of serine dehydratase activity by glucagon was due to increase in the rate of synthesis of enzyme molecules. Insulin repressed prenatal enzyme induction by glucagon and natural postnatal development of liver serine dehydratase. The possibility that glucagon and insulin participate in the enzyme development after birth is discussed.

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