Abstract
In addition to its application as a separation process, aqueous two-phase partitioning often yields information on important physical properties of proteins, replacing other more cumbersome analytical techniques. For example, aqueous two-phase partitioning can be used to measure the hydrophobicity and charge of a protein (1-3), to calculate dissociation constants between enzymes and substrates (4), to fractionate cell populations (5), or to characterize cell surfaces (6,7).
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References
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Forciniti, D. (2000). Studying the Influence of Salts on Partitioning of Proteins. In: Hatti-Kaul, R. (eds) Aqueous Two-Phase Systems: Methods and Protocols. Methods in Biotechnology™, vol 11. Humana Press. https://doi.org/10.1385/1-59259-028-4:201
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DOI: https://doi.org/10.1385/1-59259-028-4:201
Publisher Name: Humana Press
Print ISBN: 978-0-89603-541-6
Online ISBN: 978-1-59259-028-5
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