Abstract
Affinity partitioning in aqueous two-phase systems has been applied to study the interaction of serum proteins with certain dyes. By monitoring the partition coefficient any interaction between proteins and dyes and its alteration under certain conditions can easily be recognized. In detail, the binding of Cibacron Blue F3G-A and Remazol Yellow GGL to albumin and prealbumin was studied. The influence of competing ligands and of dye modification on affinity partitioning of prealbumin was demonstrated. Furthermore, affinity partitioning in three-phase systems composed of PEG, Ficoll and dextran is shown. Attempts were made to fractionate serum proteins by countercurrent distribution using polymer-bound reactive dyes.
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References
P.-A. Ålbertsson, “Partition of cell particles and macromolecules”, John Wiley & Sons, New York (1986)
H. Walter, D.E. Brooks and D. Fisher, “Partitioning in aqueous two-phase systems. Theory, methods, uses and applications to biotechnology,” Academic Press Inc., Orlando (1985)
S.D. Flanagan and S.H. Barondes, Affinity partitioning: A method for purification of proteins using specific polymer ligands in aqueous polymer two-phase systems, J. Biol. Chem. 250:1484 (1975)
G. Johansson, G. Kopperschläger and P.-A. Ålbertsson, Affinity partitioning of phosphofructokinase from baker’s yeast using polymer-bound Cibacron Blue F3G-A, Eur. J. Biochem. 131:589 (1983)
M.R. Kula, K.H. Kroner and H. Hustedt, Purification of enzymes by liquid-liquid extraction, Adv. Biochem. Eng. 24:73 (1982)
G. Birkenmeier, G. Kopperschläger and G. Johansson, Separation and studies of serum proteins with aid of aqueous two-phase systems containing dyes as affinity ligands, Biomed. Chromatogr. 1:64 (1986)
G. Kopperschläger, H.-J. Böhme and E. Hofmann, Cibacron Blue F3G-A and related dyes as ligands in affinity chromatography, in: “Advances in Biochemical Engineering”, A. Fichter, ed., Springer, Berlin (1982)
S. Subramanian, Dye-affinity chromatography: the interaction of Cibacron Blue F3G-A with proteins and enzymes, CRC Crit. Rev. Biochem. 16:169 (1984)
G. Johansson and M. Andersson, Liquid-liquid extraction of glycolytic enzymes from baker’s yeast using triazine dye ligands, J. Chromatogr. 291:175 (1984)
G. Johansson and M. Andersson, Parameters determining affinity partitioning of yeast enzymes using polymer-bound triazine dye ligands, J. Chromatogr. 303:39 (1984)
C.-B. Laurell, Quantitative estimation of proteins in agarose gel containing antibodies, Anal. Biochem. 15:45 (1966)
G. Birkenmeier, B. Tschechonien and G. Kopperschläger, Affinity chromatography and affinity partitioning of human serum prealbumin using immobilized Remazol Yellow GGL, FEBS Lett. 174:162 (1984)
A. Hartman, G. Johansson and P.-A. Ă…lbertsson, Partition of proteins in a three-phase system, Eur. J. Biochem. 46:75 (1974)
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© 1989 Plenum Press, New York
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Birkenmeier, G., Ålbertsson, PA., Kopperschläger, G. (1989). Dye Affinity Partitioning of Serum Proteins. In: Fisher, D., Sutherland, I.A. (eds) Separations Using Aqueous Phase Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5667-7_3
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DOI: https://doi.org/10.1007/978-1-4684-5667-7_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5669-1
Online ISBN: 978-1-4684-5667-7
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