The partition behaviour of human serum albumin and oxyhaemoglobin and several amino acids and small peptides was studied in the aqueous Ficoll-dextran biphasic system as a function of the ionic composition and pH. The partition coefficients of the solutes were expressed in terms of the equivalent number of CH2 groups, nCH2, and the equivalent number of carboxyl groups, m. The physical meaning of these two parameters and of the relationships found between them and pH for the proteins examined are discussed. A correlation was established between the difference in the relative hydrophobicities of the individual phases of various water-organic solvent systems and the interfacial tension, gamma 12, of the systems. It is argued that a relation of a similar type exists for the aqueous polymeric biphasic systems. The possibility of estimating the relative intensity of Van der Waals and hydration interactions of a solute and particle surface by examination of their partitioning in a biphasic system calibrated for the hydrophobic and hydration properties of the phases is discussed.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/s0021-9673(01)88211-x | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!