Abstract
The affinity of two kinases for Blue Dextran was discovered in 1968 during gel permeation chromatography (1) and agarose electrophoresis (2). The observed interaction was mediated by the chromophore of Blue Dextran, Cibacron Blue F3G-A (3), which was postulated to bind to the supersecondary structure of certain enzymes known as the dinucleotide fold (4). Immobilized Cibacron Blue F3G-A replaced more expensive biological group-specific ligands in the affinity chromatographic purification of a wide variety of nucleotide-binding enzymes (5). The adsorbent was easier to synthesize, biochemically more stable, and had much higher capacities than the traditional nucleotide-based affinity matrices, making it more suitable for large-scale purifications.
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References
Haekel, R., Hess, B., Lauterborn, W., and Winsler, K.H. (1968) Purification and allosteric poroperties of yeast pyruvate kinase. Hoppe Seylers Z. Physiol. Chem. 349, 699.
Kopperschlaeger, G., Freyer, R., Diezel, W., and Hofmann, F. (1968) Some kinetics and molecular properties of yeast phosphofructokinase. FEBS Lett. 1, 137.
Kopperschlaeger, G., Diezel, W., Freyer, R., Liebe, S., and Hofmann, F. (1971) Interaction of yeast phosphofructokinase with Blue Dextran 2000. Eur. J. Biochem. 22, 40–45.
Stellwagen, E. (1977) Use of Blue Dextran as a probe for the nicotinamide adenine dinucleotide domain in proteins. Acct. Chem. Res. 10, 92–98.
Dean, P.D.G. and Watson, D. H. (1979) Protein purification using immobilised triazine dyes. J. Chrotnatogr. 165, 301–320.
Bonnerjea, J., Oh, S., Hoare, M., and Dunnill, P. (1986) Protein purification: The right step at the right time. Bio/Technology 4, 954–958.
Qadri, F. (1985) The reactive triazine dyes: Their usefulness and limitations in protein purifications. Trends Biotechnol. 3, 7–12.
Hey, Y. and Dean, P.D.G. (1983) Tandem dye-ligand chromatography and biospecific elution applied to the purification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Biochem. J. 209, 363–371.
Scopes, R.K. (1986) Strategies for enzyme isolation using dye-ligand and related adsorbents. J. Chromatogr. 376, 131–140.
Lowe, C.R. and Pearson, J.C. (1984) Affinity chromatography on immobilised dyes. Meth. Enzymol. 104, 97–113.
Angal, S. and Dean, P.D.G. (1977) The effect of matrix on the binding of albumin to immobilized Cibacron Blue. Biochem. J. 167, 301–303.
Angal, S. and Dean, P.D.G. (1978) The use of immobilised Cibacron Blue in plasma fractionation. FEBS Lett. 96, 346–348.
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© 1988 The Humana Press Inc.
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Angal, S. (1988). Dye-Ligand Chromatography. In: Walker, J.M. (eds) New Protein Techniques. Methods in Molecular Biology™, vol 3. Humana Press. https://doi.org/10.1385/0-89603-126-8:111
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DOI: https://doi.org/10.1385/0-89603-126-8:111
Publisher Name: Humana Press
Print ISBN: 978-0-89603-126-5
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