TY - JOUR
T1 - A novel nucleolytic activity associated with rabbit liver tRNA nucleotidyltransferase
AU - Deutscher, Murray P.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1973/5/1
Y1 - 1973/5/1
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(73)90976-5
DO - 10.1016/0006-291X(73)90976-5
M3 - Article
C2 - 4351304
AN - SCOPUS:0015622515
VL - 52
SP - 216
EP - 222
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -