Purification of Leucyl Transfer Ribonucleic Acid Synthetase from Escherichia coli

Leucyl transfer ribonucleic acid synthetase (EC 6.1.1.4, l -leucine:tRNA ligase (AMP)) from Escherichia coli has been purified to near homogeneity. The molecular weight of the enzyme is approximately 105,000 and its sedimentation coefficient ( s 0 20, w ) is 5.4 S. In the presence of EDTA or in the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1970-03, Vol.245 (6), p.1401-1406
Main Authors: H. Hayashi, J. R. Knowles, Jon R. Katze, J. Lapointe, Dieter Söll
Format: Article
Language:English
Subjects:
Alkylation
Amino Acids - analysis
Chromatography
Chromatography, DEAE-Cellulose
Drug Stability
Edetic Acid
Electrophoresis
Escherichia coli - enzymology
Hydrogen-Ion Concentration
Hydroxyapatites
Leucine
Ligases - analysis
Ligases - isolation & purification
Methods
Molecular Weight
Oxidation-Reduction
RNA, Bacterial
RNA, Transfer
Sodium Chloride
Temperature
Time Factors
Ultracentrifugation
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Summary:Leucyl transfer ribonucleic acid synthetase (EC 6.1.1.4, l -leucine:tRNA ligase (AMP)) from Escherichia coli has been purified to near homogeneity. The molecular weight of the enzyme is approximately 105,000 and its sedimentation coefficient ( s 0 20, w ) is 5.4 S. In the presence of EDTA or in the absence of reducing agents, the enzyme is rapidly inactivated.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)63250-8