
The interaction of aminoacyl-tRNA synthetase with RNA and polyanions was studied. The inhibition of the enzymes by polyU, polyI and heparin was demonstrated. It was found that this interaction is of limited specificity and is typical of single-stranded RNAs which possess no orderly secondary structure as well as of other polyanions possessing similar polyelectrolytic properties. Data from kinetic analysis and lysyl-tRNA synthetase modification by pyridoxal phosphate are suggestive of participation of the tRNA binding site in the enzyme interaction with polyanions.
Lysine-tRNA Ligase, Poly U, Heparin, Polymers, Valine-tRNA Ligase, Arginine-tRNA Ligase, Polyelectrolytes, Amino Acyl-tRNA Synthetases, Kinetics, Liver, RNA, Transfer, Poly I, Animals, Rabbits
Lysine-tRNA Ligase, Poly U, Heparin, Polymers, Valine-tRNA Ligase, Arginine-tRNA Ligase, Polyelectrolytes, Amino Acyl-tRNA Synthetases, Kinetics, Liver, RNA, Transfer, Poly I, Animals, Rabbits
| 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). | 0 | |
| 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 |
