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Transfer Ribonucleic Acid Nucleotidyltransferase from Escherichia coli

II. PURIFICATION, PHYSICAL PROPERTIES, AND SUBSTRATE SPECIFICITY

From the ¹ From the Department of Biochemistry, St. Louis University School of Medicine, St. Louis, Missouri 63104

Transfer RNA nucleotidyltransferase (EC 2.7.7.25) from Escherichia coli has been purified to near homogeneity. The apparent molecular weight of the enzyme is about 50,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration. No evidence for subunits was obtained. The enzyme is rapidly and irreversibly inactivated in the absence of magnesium. The enzyme incorporates only 1 AMP and 2 CMP residues into tRNA from which the terminal -pC-C-A had been removed. All E. coli amino acid acceptor tRNA species as well as heterologous tRNA can serve as substrates.

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