Abstract
The reaction of polyuridylic acid with sodium bisulfite produces modified polymers in which up to 95% of the uracil residues have been converted to uracil-6-sulfonate residues. A 91.6% bisulfite-saturated polymer was found to resist hydrolysis by spleen phosphodiesterase and phosphorolysis by polynucleotide phosphorylase. Digestion by pancreatic ribonuclease was successful and gave the bisulfite adduct of uridine-3′-phosphate. Treatment of this nucleotide adduct with acid phosphatase afforded the bisulfite adduct of uridine. The ability of polyuridylic acid to bind to ribosomes, and to stimulate the binding of phenylalanine tRNA to ribosomes was abolished by progressive bisulfite saturation of the polymer. The rate of decline of these functionsf with increasing bisulfite content, was less sharp than the loss of phenyl-alanine coding ability o, the modified polymer.
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Shapiro, R., Braverman, B. & Szer, W. Modification of polyuridylic acid by bisulfite. II: Studies on ribosomal binding and enzymatic hydrolysis. Molecular Biology Reports 1, 123–127 (1973). https://doi.org/10.1007/BF00357592
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DOI: https://doi.org/10.1007/BF00357592