Co-purification of coenzyme-dependent enzymes by affinity chromatography

Recent developments in general ligand affinity chromatography have greatly facilitated the purification of numerous coenzyme-dependent enzymes in practical scale. By immobilizing various derivatives of coenzymes (NAD+, NADP+, ATP and coenzyme A) on Sepharose, these general ligand affinity columns ha...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1983-01, Vol.57 (1), p.27-40
Main Author: LEE, C.-Y. G
Format: Article
Language:English
Subjects:
affinity chromatography
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Biotechnology
Chemical Phenomena
Chemistry
Chromatography, Affinity - methods
Coenzymes
Drosophila - enzymology
Enzyme engineering
enzymes
Enzymes - isolation & purification
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Hexokinase - isolation & purification
Improved methods for extraction and purification of enzymes
Isoenzymes - isolation & purification
L-Lactate Dehydrogenase - isolation & purification
Ligands
Methods. Procedures. Technologies
Mice
Phosphoglycerate Kinase - isolation & purification
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Summary:Recent developments in general ligand affinity chromatography have greatly facilitated the purification of numerous coenzyme-dependent enzymes in practical scale. By immobilizing various derivatives of coenzymes (NAD+, NADP+, ATP and coenzyme A) on Sepharose, these general ligand affinity columns have the potential of enriching as many as 30% of the two thousand known enzymes as well as their isozymic forms, if they are applied in combination with the conventional procedures.
ISSN:0300-8177
1573-4919
DOI:10.1007/BF00223522