Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus.
A nucleoside triphosphate phosphohydrolase activity has been discovered in reovirus virions. This activity converts nucleoside triphosphates to nucleoside diphosphates in vitro. Properties of this enzyme are presented, with evidence that this activity is an integral part of the virion core.
D000818:Animals; D002499:Centrifugation, Density Gradient; D002855:Chromatography, Thin Layer; D006863:Hydrogen-Ion Concentration; D007739:L Cells; D008094:Lithium / Q000494:pharmacology; D008274:Magnesium; D051379:Mice; D010042:Ouabain / Q000494:pharmacology; D010710:Phosphates / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000494:pharmacology; D012316:RNA Nucleotidyltransferases / Q000378:metabolism; D012087:Reoviridae / Q000201:enzymology*; D012964:Sodium / Q000494:pharmacology; D014316:Tritium; D014529:Uridine / Q000378:metabolism
D010710:Phosphates; D014316:Tritium; D010042:Ouabain; D008094:Lithium; D012964:Sodium; D012316:RNA Nucleotidyltransferases; D010744:Phosphoric Monoester Hydrolases; D008274:Magnesium; D011188:Potassium; D014529:Uridine