Abstract
Partitioning in aqueous polymer two-phase systems is widely recognized as a highly efficient, versatile, and cost-effective method for separation and purification of biological materials.1-6 Aqueous two-phase systems arise in aqueous mixtures of different water-soluble polymers or a single polymer and a specific salt. When two certain polymers, e.g., dextran and polyethylene glycol are mixed in water above certain concentrations, the mixture separates into two immiscible aqueous phases. There is a clear interfacial boundary and one phase is rich in one polymer and the other phase is rich in the other. The aqueous solvent in both phases provides media suitable for biological products.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
P.Å. Albertsson. “Partition of Cell Particles and Macromolecules,” 3rd. ed., Wiley, New York (1986).
“Partitioning in Aqueous Two-Phase Systems. Theory, Methods, Uses, and Applications to Biotechnology,” H. Walter, D.E. Brooks, D. Fisher, eds., Academic Press, Orlando, Florida (1985).
W. Muller. “Liquid-Liquid Partition Chromatography of Biopolymers,” GIT Verlag, Darmstadt (1988).
“Separations Using Aqueous Phase Systems. Applications in Cell Biology and Biotechnology,” D. Fisher and I.A. Sutherland, eds., Plenum Press, New York (1989).
“Methods in Enzymology, Vol. 228, Aqueous Two-Phase Systems,” H. Walter and G. Johansson, eds., Academic Press, Orlando, Florida (1994).
B.Y. Zaslaysky. “Partitioning in Aqueous Two-Phase Systems: Physical Chemistry and Bioanalytical Applications,” Marcel Dekker, New York (1994).
F.D. Raymond, D.W. Moss, and D. Fisher, Phase partitioning detects differences between phospholipasereleased forms of alkaline phosphatase - a GPI-linked protein, Biochim. Biophys. Acta 1156:117 (1993).
A.D. Diamond, K. Yu, and J.T. Hsu, The effect of amino acid sequence on peptide and protein partitioning in aqueous two-phase systems, in: “Protein Purification: From Molecular Mechanisms to Large-Scale Processes,” M.R. Ladisch, R.C. Willson, C.C. Painton, and S.E. Builder, eds., ACS Symposium Series, Vol. 427, pp. 52–65, American Chemical Society, Washington, D.C. (1990).
V.V. Mozhaev, V.A. Siksnis, N. S. Melik-Nubarov, N.Z. Galkantaite, G.J. Denis, E.P. Butkus, B.Y. Zaslaysky, N.M. Mestechkina, and K. Martinek, Protein stabilization via hydrophilization. Covalent modification of trypsin and α-chymotrypsin, Eur. J. Biochem. 173:147 (1988).
S.-O. Enfors, K. Köhler, and A. Veide, Combined use of extraction and genetic engineering for protein purification: recovery of (β-galactosidase fused proteins, Bioseparation 1:305 (1990).
J.R. Luther and C.E. Glatz, Genetically engineered charge modifications to enhance protein separation in aqueous two-phase systems: electrochemical partitioning, Biotechnol. Bioeng. 44:147 (1994).
H. Tanaka, R. Kuboi, and I. Komasawa, The effect of hydrochloric acid on hydrophobicity and partition of protein in aqueous two-phase systems, J. Chem. Eng. Jpn. 24:661 (1991).
R. Kuboi, K. Yano, H. Tanaka, and I. Komasawa, Evaluation of surface hydrophobicities during refolding process of carbonic anhydrase using aqueous two-phase partitioning systems, J. Chem. Eng. Jpn. 26:286 (1993).
B.Y. Zaslaysky, N.M. Mestechkina, L.M. Miheeva, and S.V. Rogozhin, Measurements of relative hydrophobicity of amino acid side-chains by partition in an aqueous two-phase polymeric system: hydrophobicity scale for non-polar and ionogenic side-chains, J. Chromatogr. 240:21 (1982).
B.Y. Zaslaysky and E.A. Masimov, Methods of analysis of the relative hydrophobicity of biological solutes, Topics Curr. Chem. 146:171 (1988).
B.Y. Zaslaysky, A.A. Borovskaya, N.D. Gulaeva, and L.M. Miheeva, Partitioning in aqueous two-phase systems as a method of estimation of the relative hydrophobicity of solutes, J. Chem. Soc. Faraday Trans. 87:137 (1991).
P.A. Rebinder, Hydrophilicity and hydrophobicity, in: “Kratkaya Khimicheskaya Encyclopedia,” Vol.1, p. 937, Sovetskaya Encyclopedia, Moscow (1961).
C. Hansch and A. Leo. “Substituent Constants for Correlation Analysis in Chemistry and Biology,” Academic Press, New York (1979).
R. Franke. “Theoretical Drug Design Methods”, Elsevier, Amsterdam (1984).
B.Y. Zaslaysky, N.M. Mestechkina, L.M. Miheeva, S.V. Rogozhin, G.Y. Bakalkin, G.G. Rjazhsky, E.V. Chetverina, A.A. Asmuko, J.D. Bespalova, N.V. Korobov, and O.N. Chichenkov, Correlation of hydrophobic character of opioid peptides with their biological activity measured in various bioassay systems, Biochem. Pharmacol. 31:3757 (1982).
N.D. Gulaeva, I.A. Yamskov, and B.Y. Zaslaysky, unpublished data (1990).
N.D. Gulaeva and B.Y. Zaslaysky, unpublished data (1990).
N.D. Gulaeva, M.A. Chlenov, B.Y. Zaslaysky, unpublished data (1989).
A.F. Bristow and S.L. Jeffcoate, Analysis of therapeutic growth hormone preparations: report of an interlaboratory collaborative study on growth hormone assay methodologies, Biologicals 20:221 (1992).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Zaslavsky, B.Y. (1995). Use of the Aqueous Two-Phase Partition Technique for Characterization and Quality Control of Recombinant Proteins. In: Rogers, R.D., Eiteman, M.A. (eds) Aqueous Biphasic Separations. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1953-9_15
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1953-9_15
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5802-2
Online ISBN: 978-1-4615-1953-9
eBook Packages: Springer Book Archive