Enzymatic polymerization of 5-mercuriuridine-5'-diphosphate with polynucleotide phosphorylase from E. coli

We report the polymerization of 5-mercuriuridine-5'-diphosphate (ppUHgX), in the presence of an excess of beta-mercaptoethanol, with polynucleotide phosphorylase from E. coli. A degradation of mercurated nucleotides with mercaptans was observed and about 30% of incorporation of mercury in the polymer was obtained after treatment with pancreatic RNase. The influence of ppUHgX and pUHgX with or without beta-mercaptoethanol was also studied on the polymerization of UDP. The ppUHgX did not polymerize in the absence of beta-mercaptoethanol.