Determination of dissociation constants for binary dehydrogenase-coenzyme complexes by (Bio)affinity chromatography on an immobilized AMP-analogue
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference25 articles.
1. General ligands in affinity chromatography. Cofactor–substrate elution of enzymes bound to the immobilized nucleotides adenosine 5′-monophosphate and nicotinamide–adenine dinucleotide
2. Affinity chromatography of enzymes on an AMP-analogue: Specific elution of dehydrogenases from a general ligand
3. Separation of the isoenzymes of lactate dehydrogenase by affinity chromatography using an immobilized AMP-analogue
4. Separation of Isozymes of horse liver alcohol dehydrogenase and purification of the enzyme by affinity chromatography on an immobilized AMP-analogue
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1. Determination of binding constants between one protein and multiple carbohydrates by affinity chromatography on a microchip;Journal of Chromatography A;2012-12
2. Immobilized Coenzymes in General Ligand Affinity Chromatography and Their Use as Active Coenzymes;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Glutamate Dehydrogenase from Peas: Isolation, Quaternary Structure, and Influence of Cations on Activity;European Journal of Biochemistry;2005-03-03
4. Utilization of enzyme–substrate interactions in analytical chemistry;Journal of Chromatography B: Biomedical Sciences and Applications;1999-02
5. Thin-Layer Affinity Chromatography in Analysis of Protein–Ligand Affinity;Analytical Biochemistry;1996-12
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