Effect of insulin on mitochondrial oxidative phosphorylation and energy charge of the perfused guinea pig liver.
The effect of insulin was investigated in the isolated guinea pig liver perfused with Krebs-Ringer bicarbonate buffer containing red blood cells and albumin. In the mitochondria isolated from livers perfused with 10 units of insulin per hour, the phosphorylative activity with glutamate as a substrate increased to about 160 per cent of control 60 minutes after the beginning of perfusion (p less than 0.01). Such an enhanced phosphorylative activity was accompanied by increases in the respiratory control ratio, state 3 respiration, and P/O ratio. On the other hand, in the liver perfused with insulin, the levels of the energy charge and adenine nucleotide quotient increased to a significant degree as compared to the liver without insulin (p less than 0.01 and p less than 0.05, respectively). It is suggested that insulin plays an important role as a portal factor in regulating mitochondrial oxidative phosphorylation and the levels of the phosphorylated adenine nucleotides.
Effect of insulin on mitochondrial oxidative phosphorylation and energy charge of the perfused guinea pig liver. The effect of insulin was investigated in the isolated guinea pig liver perfused with Krebs-Ringer bicarbonate buffer containing red blood cells and albumin. In the mitochondria isolated from livers perfused with 10 units of insulin per hour, the phosphorylative activity with glutamate as a substrate increased to about 160 per cent of control 60 minutes after the beginning of perfusion (p less than 0.01). Such an enhanced phosphorylative activity was accompanied by increases in the respiratory control ratio, state 3 respiration, and P/O ratio. On the other hand, in the liver perfused with insulin, the levels of the energy charge and adenine nucleotide quotient increased to a significant degree as compared to the liver without insulin (p less than 0.01 and p less than 0.05, respectively). It is suggested that insulin plays an important role as a portal factor in regulating mitochondrial oxidative phosphorylation and the levels of the phosphorylated adenine nucleotides.