Studies on fish liver protein synthesis. II. Factors influencing the aminoacylation of shark liver transfer ribonucleic acid.
The influence of buffer, pH, Mg2+, ATP, Na+, K+ and temperature on the extent and rate of aminoacyl-tRNA synthesis was studied with the shark Mustelus mento liver tRNAs and aminoacyl-tRNA synthetases. The optimum pH for the aminoacylation of tRNAMet was 8.3 and for tRNAVal 7.0. For these two tRNAs the Mg2+ optimum was related to the levels of ATP required and to the pH of the reactions. It is suggested that the Mg2+ concentration required for each aminoacylation system reflects the true conditions under which the substrate for the enzyme, the MgATP2- complex, is formed. The effect of monovalent cations was also examined. Val-tRNA synthesis was slightly stimulated up to a concentration of 50 mM NaCl (KCl). Over 100 mM salt, a rapid inhibition was observed. Met-tRNA synthesis behaves differently by being stimulated over a wide range of salt concentrations.
Studies on fish liver protein synthesis. II. Factors influencing the aminoacylation of shark liver transfer ribonucleic acid. The influence of buffer, pH, Mg2+, ATP, Na+, K+ and temperature on the extent and rate of aminoacyl-tRNA synthesis was studied with the shark Mustelus mento liver tRNAs and aminoacyl-tRNA synthetases. The optimum pH for the aminoacylation of tRNAMet was 8.3 and for tRNAVal 7.0. For these two tRNAs the Mg2+ optimum was related to the levels of ATP required and to the pH of the reactions. It is suggested that the Mg2+ concentration required for each aminoacylation system reflects the true conditions under which the substrate for the enzyme, the MgATP2- complex, is formed. The effect of monovalent cations was also examined. Val-tRNA synthesis was slightly stimulated up to a concentration of 50 mM NaCl (KCl). Over 100 mM salt, a rapid inhibition was observed. Met-tRNA synthesis behaves differently by being stimulated over a wide range of salt concentrations.