Affinity Chromatography of Glyceraldehyde-3-phosphate Dehydrogenase. A Comparative Study of the Enzymes from Yeast and Sturgeon Muscle
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1977.tb11741.x/fullpdf
Reference37 articles.
1. Affinity chromatography of enzymes on insolubilized cofactors
2. Purification of nicotinamide-adenine dinucleotide-dependent dehydrogenases by affinity chromatography
3. General ligands in affinity chromatography. Cofactor–substrate elution of enzymes bound to the immobilized nucleotides adenosine 5′-monophosphate and nicotinamide–adenine dinucleotide
4. Affinity chromatography of nicotinamide–adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide
5. Affinity chromatography of nicotinamide nucleotide-dependent dehydrogenases on immobilized nucleotide derivatives
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1. Chapter 9 Bioaffinity Chromatography in the Isolation, Determination or Removal of Biologically Active Substances;Bioaffinity Chromatography;1993
2. Specific purification of glyceraldehyde-3-phosphate dehydrogenase by hydrophobic chromatography on immobilized colchicine;Biochimica et Biophysica Acta (BBA) - General Subjects;1989-04
3. Review : Polymeric Biomaterials As Enzyme and Drug Carriers Part II: Immobilization of Coenzymes and Other Biological Components;Journal of Bioactive and Compatible Polymers;1988-10
4. Interaction of glyceraldehyde-3-phosphate dehydrogenase with the cytoplasmic pole of band 3 from bovine erythrocyte membrane: The mode of association and identification of the binding site of band 3 polypeptide;Archives of Biochemistry and Biophysics;1987-08
5. Étude immunologique de la glycéraldéhyde-3-phosphate-déshydrogénase chez les entérobactéries; intérêt taxonomique;Annales de l'Institut Pasteur / Microbiologie;1983-03
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