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dc.contributor.advisorJames Manion
dc.contributor.advisorJohn Christenson
dc.contributor.advisorKenneth Watson
dc.contributor.authorDougherty, Sarsfield
dc.contributor.authorHarrington, Daniel
dc.date.accessioned2020-04-30T10:03:21Z
dc.date.available2020-04-30T10:03:21Z
dc.date.issued1982-04-01
dc.identifier.urihttps://scholars.carroll.edu/handle/20.500.12647/3194
dc.description.abstractTwo enzymes, one which catalyzes the addition of one or more cytidine 5'-monophosphate residue from cytidine 5’-triphosphate to the 3'-terminus of a ribonucleic acid primer, referred to as ribocytidylyl terminal transferase, and one which catalyzes the addition of one or more uridine 5’-monophosphate residue from uridine 5'-triphosphate to the 3'-terminus of a ribonucleic acid primer, referred to as ribouridylyl terminal transferase, have been purified from RNA tumor virus-infected avian myeloblasts. The purification procedure involved cation and anion exchange chromatography. Both enzymes were stimulated by the divalent cations Mg++ and Mn++ with optimal concentrations of 0.0001 M Mn++ and between 0.001 M and 0.004 M Mg++. The molecular weight of ribocytidylyl terminal transferase was approximately 60,000 and the molecular weight of ribouridylyl terminal transferase was approximately 56,000.
dc.titlePurification And Characterization Of Ribouridylyl Terminal Transferase And Ribocytidylyl Terminal Transferase Activities From RNA Tumor Virus-Infected Avian Myeloblasts
dc.typethesis
carrollscholars.object.degreeBachelor's
carrollscholars.object.departmentLife & Environmental Sciences
carrollscholars.object.disciplinesBiochemistry
carrollscholars.legacy.itemurlhttps://scholars.carroll.edu/lifesci_theses/452
carrollscholars.legacy.contextkey12520306
carrollscholars.object.seasonSpring
dc.date.embargo12/31/1899 0:00


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