Isolation of a single polypeptide leucyl-tRNA synthetase from bakers' yeast1
- 1 January 1979
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 6 (11) , 3651-3660
- https://doi.org/10.1093/nar/6.11.3651
Abstract
A single polypeptide of leucyl-tRNA synthetase (LRS) has been purified from budding bakers' yeast by a modification of the procedure published earlier. On denaturing polyacrylamide gel electrophoresis LRS was one band corresponding to molecular weight of 120,000 +/- 5,000 daltons. Variable amounts of LRS with a similar molecular weight but which dissociated into equal subunits of 58,000 were also isolated. The affinities (KM) for substrates for this form of the enzyme were similar to those previously reported for the dimeric form of the enzyme.Keywords
This publication has 18 references indexed in Scilit:
- Complete purification and studies on the structural and kinetic properties of two forms of yeast valyl-tRNA synthetaseBiochimie, 1976
- Kinetic studies of leucyl transfer RNA synthetase from bakers' yeast. Order of addition of substrates and release of products.Journal of Biological Chemistry, 1975
- Multiple Forms of Tryptophanyl‐tRNA Synthetase from Beef PancreasEuropean Journal of Biochemistry, 1975
- Purification of Tyrosine: tRNA Ligase from Saccharomyces cerevisiae αS288CThe Journal of Biochemistry, 1973
- Purification and properties of leucyl-tRNA synthetase from Bakers' yeast.1973
- The Subunit Structure of Tryptophanyl Transfer Ribonucleic Acid Synthetase from Beef PancreasJournal of Biological Chemistry, 1972
- Yeast phenylalanyl transfer ribonucleic acid synthetase. Purification, molecular weight, and subunit structureBiochemistry, 1971
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein MixturesJournal of Biological Chemistry, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951