Download Aqueous Biphasic Separations: Biomolecules to Metal Ions by Robin D. Rogers, Andrew H. Bond, Cary B. Bauer (auth.), PDF

By Robin D. Rogers, Andrew H. Bond, Cary B. Bauer (auth.), Robin D. Rogers, Mark A. Eiteman (eds.)

''A grand compilation...Well-bound, well-printed....It is certain that this pioneering ebook can help transforming into curiosity of the separation scientists in aqueous biphasic structures and develop the scope of the field.'' --- Indian Chemical Society, 1998

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Additional info for Aqueous Biphasic Separations: Biomolecules to Metal Ions

Example text

In general, these models suffer from a lack of appropriate experimental data from the numerous possible systems to determine values for the various model parameters. The models often do not simplify the daunting task of selecting for a particular application a system from among the numerous possibilities, In contrast to predicting the binodal, the goal of a second type of model is to predict the partition coefficient. Fortunately, the same thermodynamic models used to predict the binodal can often be extended to the prediction of a solute's partition coefficient.

The results are what is commonly observed in other PEG/salt systems. 0 system), the tie-line length is greater for the more basic system. In other words, the binodal extends closer to the zero concentration axes the higher the pH. This is true when the concentration axes are written on a weight basis or on a mole basis. Of course, considering Equation 1 these observations suggest that the partition coefficient of any solute will change with changing pH, merely because changing pH alters the phase diagram.

Ratio. A salt with two ions that have very different affinities for the two phases will generate a larger potential difference than a salt with ions that have similar affinities for the phases. It can be shown that, in the presence of excess of salt, a protein will partition according to: In K p = K; + (FZ/RT)'" (4) where Kp is the partition coefficient of the protein and K; is the value of this coefficient when the interfacial potential (generated by the excess salt) is zero or when the protein net charge Z is zero.

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