Inhibition of protein synthesis by (aminooxy)acetate in rat liver

(Aminooxy)acetate and D-cycloserine, two inhibitors of hepatic transamination reactions, inhibited also protein synthesis in isolated cells and postmitochondrial supernatants from rat liver. Both inhibitors acted in extracts only in concentrations higher than 1 mM. However, while D-cycloserine acted in isolated cells, as in extracts, (aminooxy)acetate inhibits protein synthesis in isolated cells by 50% of the control in the range 0.03-3 mM. NH+4 and H2O2, two by-products of (aminooxy)acetate degradation, inhibited protein synthesis in isolated liver cells, but at such a high concentration that the inhibition of protein synthesis carried out by (aminooxy)acetate cannot be explained by generation of these species. The results point out that the inhibitory action of (aminooxy)acetate on protein synthesis appears to require the integrity of the molecule.