Purification of aspartase and aspartokinase-homoserine dehydrogenase I from Escherichia coli by dye-ligand chromatography

Improved purification schemes are reported for the enzymes l-aspartase and aspartokinase-homoserine dehydrogenase I from Escherichia coli. Dye-ligand chromatography on commercially available dye matrices are incorporated as key steps in these purifications. Red A-agarose has a high affinity for l-as...

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Veröffentlicht in:	Analytical biochemistry 1985-01, Vol.147 (2), p.336-341
Hauptverfasser:	Karsten, William E., Hunsley, James R., Viola, Ronald E.
Format:	Artikel
Sprache:	eng
Schlagworte:	affinity chromatography Ammonia-Lyases - isolation & purification Analytical, structural and metabolic biochemistry aspartate ammonia-lyase Aspartate Ammonia-Lyase - isolation & purification aspartate kinase Aspartokinase Homoserine Dehydrogenase - isolation & purification Biological and medical sciences Chromatography, Affinity - methods Chromatography, Agarose Chromatography, DEAE-Cellulose Coloring Agents enzyme Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology homoserine dehydrogenase kinase lyase Lyases Multienzyme Complexes - isolation & purification
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