Investigation of affinity partition chromatography using formate dehydrogenase as a model.
The enzyme formate dehydrogenase (FDH) was purified from the crude extract of Candida boidinii by affinity partition chromatography. The partition coefficient, K, of the enzyme was selectively increased by adding polyethylene glycol-Procion Red HE3b as an affinity ligand to the mobile phase in the chromatographic column. The increased K value led to early elution of the enzyme-ligand complex and separated the target protein from the main peak of the contaminants.
Walsdorf
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Institut für Enzymtechnologie der Heinrich Heine Universität Düsseldorf, Jülich, F.R.G.
Forciniti
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D002175:Candida / Q000201:enzymology*; D002846:Chromatography, Affinity / Q000379:methods*; D005560:Formate Dehydrogenases / Q000032:analysis*; D008024:Ligands; D008956:Models, Chemical; D014227:Triazines
D008024:Ligands; D014227:Triazines; C020795:procion red HE-3B; D005560:Formate Dehydrogenases