Abstract
This paper investigates means of obtaining selective affinity for specific target proteins in aqueous two-phase systems. This can be achieved by exploiting specific properties of the protein such as biological affinity. By using specific salts (eg. NaCl) the charge and hydrophobic properties of the proteins can be exploited thus changing the partition between the two phases quite dramatically.
Finally our present work on chemical protein modification to study the effect of individual protein properties is described. This will allow the development of appropriate correlations that can be used for prediction of protein behaviour in aqueous two-phase systems.
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Franco, T., Andrews, B.A., Cascone, O., Hodgson, C., Andrews, A.T., Asenjo, J.A. (1990). Affinity Separation of Proteins in Aqueous Two-Phase Systems. In: Pyle, D.L. (eds) Separations for Biotechnology 2. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0783-6_36
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DOI: https://doi.org/10.1007/978-94-009-0783-6_36
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6839-0
Online ISBN: 978-94-009-0783-6
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