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PMID: 6362667 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Large scale purification and structural properties of yeast aspartyl-tRNA synthetase.

Biochemical and biophysical research communications ·Vol. 117 ·No. 1 ·1983-11-30 ·Pages 259-67

Lorber B, Kern D, Dietrich A, Gangloff J, Ebel JP, Giegé R

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.

MeSH Terms
Amino Acyl-tRNA Synthetases/isolation & purification Aspartate-tRNA Ligase/isolation & purification,metabolism Crystallization Macromolecular Substances Molecular Weight Protein Conformation Saccharomyces cerevisiae/enzymology
Chemicals
Macromolecular Substances Amino Acyl-tRNA Synthetases Aspartate-tRNA Ligase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lorber B
Kern D
Dietrich A
Gangloff J
Ebel J P
Giegé R
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1983-11-30
Pages
259-67
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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