Increase in the adenine nucleotide translocase protein contributes to the perinatal maturation of respiration in rat liver mitochondria.

An assay based on the high-affinity binding of tritium-labelled atractyloside to the adenine nucleotide translocase (ANT) was developed for estimation of its content in samples of mitochondria, cells and tissue homogenate. The assay was used to study the developmental change of the ANT protein concentration in perinatal rat liver. Within the last 3 days before birth the content of the ANT protein per mg tissue protein increased from 29 to 45% of the maximum value found 2 days after birth. A similar developmental change of the ANT protein was found in isolated mitochondria, demonstrating that the perinatal increase in the ANT protein content was due mainly to a mitochondrial differentiation process and not the result of an increase in the number of mitochondria per cell. A close proportionality between the ANT protein and the ADP-stimulated respiration of liver homogenate was found in the perinatal period from 3 days before to 2 days after birth. This finding suggests that the developmental change in the ANT protein content plays an important role in the onset of oxidative phosphorylation after birth.