PURIFICATION AND PROPERTIES OF TRANSFER-RNA(ADENINE-1)-METHYLTRANSFERASE FROM RAT-LIVER
- 1 January 1977
- journal article
- research article
- Vol. 252 (14) , 4790-4795
Abstract
An S-adenosylmethionine-dependent tRNA(adenine-1)-methyltransferase was purified 8000-fold from rat liver. This preparation gives a single band on polyacrylamide gel electrophoresis and is stable in long term storage. The enzyme has a MW of approximately 95,000. The single methylating capacity of this adenine-1-methyltransferase, using Escherichia coli .**GRAPHIC**. is methylation of the invariant adenine in the GT.PSI.C loop. The methylation reaction is dependent on added cation of 20-40 mM putrescine being most effective. The Km for S-adenosylmethionine was 0.3 .mu.M, while the Ki for the product inhibitor S-adenosylhomocysteine was 0.85 .mu.M. The Km for .**GRAPHIC**. is 12 nM, while that for .**GRAPHIC**. is 33 nM.This publication has 5 references indexed in Scilit:
- Physical studies of denatured tRNA2Glu from Escherichia coli.Proceedings of the National Academy of Sciences, 1976
- tRNA methyltransferases from rat liver. Differences in response of partially purified enzymes to polyamines and inorganic saltsBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
- Specificity of transfer ribonucleic acid methylases from rat liverBiochemistry, 1968
- STUDIES ON POLYNUCLEOTIDES .41. PURIFICATION OF PHENYLALANINE-SPECIFIC TRANSFER RIBONUCLEIC ACID FROM YEAST BY COUNTERCURRENT DISTRIBUTION1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951