Purification of valyl‐tRNA synthetase high‐molecular‐mass complex from rabbit liver
- 17 August 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 220 (2) , 363-365
- https://doi.org/10.1016/0014-5793(87)80847-5
Abstract
A high-molecular-mass complex containing valyl-tRNA synthetase has been purified to homogeneity from rabbit liver. The molecular mass of the complex is about 800 kDa. The complex consists of four polypeptides of 130, 50, 40 and 30 kDa.Keywords
This publication has 9 references indexed in Scilit:
- Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryoticBiochemical Journal, 1986
- Structural interpretation of low‐temperature heme‐ligand recombination rates in myoglobinFEBS Letters, 1985
- A complex from cultured Chinese hamster ovary cells containing nine aminoacyl‐tRNA synthetasesEuropean Journal of Biochemistry, 1985
- Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. III. Assignment of aminoacyl-tRNA synthetase activities to the polypeptide components of the complexes.Published by Elsevier ,1982
- High molecular mass amino acyl‐tRNA synthetase complexes in eukaryotesFEBS Letters, 1982
- Complete purification and studies on the structural and kinetic properties of two forms of yeast valyl-tRNA synthetaseBiochimie, 1976
- Affinity Elution as a Purification Method for Aminoacyl‐tRNA SynthetasesEuropean Journal of Biochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970