Abstract
Abstract Horseradish peroxidase in the presence of hydrogen peroxide selectively inactivates the amino acid acceptor activity of certain Escherichia coli transfer ribonucleic acids. Lysine acceptor activity was inactivated to the largest extent by the peroxidase treatment. Acceptor activity for isoleucine, tyrosine, histidine, and alanine was also affected, but to a lesser extent. Amino acid acceptor activity of six other amino acids tested was unaffected. The acceptor activity of rat liver transfer ribonucleic acids for all amino acids tested was insensitive to the peroxidase treatment. The peroxidase treatment did not appear to inactivate the functional sites required for lysyl transfer from E. coli transfer ribonucleic acid into polypeptide linkages in the presence of polyadenylic acid and a bacterial ribosomal system. Ultra-violet irradiation, unlike peroxidase treatment, inactivated to different extents various amino acid acceptor activities of cytoplasmic soluble ribonucleic acids from either E. coli or rat liver.
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