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


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



Biochemical and Biophysical Research Communications 117(1): 259-267



ISSN/ISBN: 0006-291X

PMID: 6362667

DOI: 10.1016/0006-291x(83)91569-3

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.

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Accession: 016250713

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Related references

Studies on aspartyl-tRNA synthetase from baker's yeast. I. Purification and properties of the enzyme. Biochimica et Biophysica Acta 294(2): 263-272, 1973

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