Effect of electrostatic energy on partitioning of proteins in aqueous two-phase systems.
An attempt has been made to adopt a different approach to evaluate the effect of a protein's charge on its partitioning behaviour in PEG/salt aqueous two-phase systems (ATPS). This has been done using a computer methodology (DelPhi) that allows the calculation of the electrostatic solvation energy that charged proteins present in a particular media such as aqueous polymer-salt systems. This calculation was done for the protein in each of the phases and a correlation was investigated that related the electrostatic energy difference of the protein in each of the phases and its partition coefficient in ATPS. Such correlation resulted in a statistical model that also included the effect of molecular weight and a shape factor at each particular pH. A global correlation which included the effect of pH was also found. All the correlations were statistically evaluated and gave good results.
Olivera-Nappa
A
A
Department of Chemical Engineering, Millenium Institute for Advanced Studies in Cell Biology and Biotechnology, University of Chile, Beauchef 861, Santiago, Chile.
Lagomarsino
G
G
Andrews
B A
BA
Asenjo
J A
JA
D002853:Chromatography, Liquid / Q000379:methods*; D003697:Delphi Technique; D055672:Static Electricity