Abstract
The inhibition of the poly U directed polyphenylalanine synthesis by gougerotin in E. coli cell free system decreased as the univalent ion (K+ or NH4+) concentration increased. At higher ion concentrations, gougerotin stimulated the polyphenylalanine synthesis. The analysis of the polyphenylalanine formed revealed that, the number of peptide chains increased in the presence of gougerotin, although gougerotin produced short peptides compared with that formed in its absence.
Some lag period was necessary before gougerotin exhibited its stimulative effect on polyphenylalanine synthesis. The reaction mixture containing 0.5M NH4Cl-washed-ribosomes showed much greater stimulation than that contained sucrose-washed-ribo-somes.
The possible explanation for this enhancement of polyphenylalanine synthesis is discussed.
