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Large scale purification and structural properties of yeast aspartyl-tRNA synthetase
- Source :
- Biochemical and biophysical research communications. 117(1)
- Publication Year :
- 1983
-
Abstract
- A large scale purification procedure of baker's yeast aspartyl-tRNA synthetase is described which yields more than 200 mg pure protein starting from 30 Kg of wet commercial cells. The synthetase is an alpha 2 dimer of Mr = 125,000 +/- 5,000 which can be crystallized (J. Mol. Biol. 138, 1980, 129-135). The enzyme has an elongated shape with a Stokes radius of 50 A and a frictional ratio of 1.5. The synthetase has a tendency to aggregate but methods are described where this effect is overcome.
- Subjects :
- Macromolecular Substances
Protein Conformation
Dimer
Aspartate—tRNA ligase
Saccharomyces cerevisiae
Aspartate-tRNA Ligase
Biophysics
Biochemistry
Amino Acyl-tRNA Synthetases
chemistry.chemical_compound
Protein structure
Molecular Biology
Stokes radius
chemistry.chemical_classification
biology
Chemistry
Cell Biology
biology.organism_classification
Yeast
Molecular Weight
Crystallography
Enzyme
biology.protein
Crystallization
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 117
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....3d68d182510fc48ece3767b1294d24c3