
pmid: 4351304
Purified preparations of rabbit liver tRNA nucleotidyltransferase contain a nucleolytic activity which removes terminal CMP residues from tRNA-C-C and tRNA-C-C-C. Other tRNA molecules, such as tRNA-C-C-A, tRNA-C-A, tRNA-C-U and tRNA-C are not substrates for this reaction. The activity exhibits a sharp optimum at about pH 10 and a divalent cation (Mg++ or Mn++) is required. The reaction is inhibited by ATP, CTP, pyrophosphate and potassium chloride. The relation of this activity to other reactions catalyzed by tRNA nucleotidyltransferase is discussed.
Diphosphates, Carbon Isotopes, Kinetics, Liver, RNA, Transfer, Animals, RNA Nucleotidyltransferases, Rabbits, Hydrogen-Ion Concentration
Diphosphates, Carbon Isotopes, Kinetics, Liver, RNA, Transfer, Animals, RNA Nucleotidyltransferases, Rabbits, Hydrogen-Ion Concentration
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 4 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
