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

Authors :
Jean-Pierre Ebel
Jean Gangloff
André Dietrich
D. Kern
Bernard Lorber
Richard Giegé
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.

Details

ISSN :
0006291X
Volume :
117
Issue :
1
Database :
OpenAIRE
Journal :
Biochemical and biophysical research communications
Accession number :
edsair.doi.dedup.....3d68d182510fc48ece3767b1294d24c3