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.
D002855:Chromatography, Thin Layer; D004926:Escherichia coli / Q000201:enzymology; D009941:Organomercury Compounds / Q000378:metabolism*; D011072:Poly U / Q000378:metabolism; D011108:Polymers / Q000378:metabolism; D011117:Polyribonucleotide Nucleotidyltransferase / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism; D014500:Uracil Nucleotides; D014530:Uridine Diphosphate / Q000378:metabolism; D014544:Uridine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism
D009941:Organomercury Compounds; D011108:Polymers; D014500:Uracil Nucleotides; D011072:Poly U; C035548:5'-mercuriuridine triphosphate; D014530:Uridine Diphosphate; D011117:Polyribonucleotide Nucleotidyltransferase; D012260:Ribonucleases; D014544:Uridine Triphosphate