Relative hydrophobicity of organic compounds measured by partitioning in aqueous two-phase systems

Features of partitioning pattern of two pancreatic enzymatic precursors: Trypsinogen and chymotrypsinogen in polyethyleneglycol–sodium citrate aqueous biphasic systems

“…Previous works have demonstrated that protein partitioning behaviour is sensitive to the surface hydrophobicity [22,10]. A high hydrophobic character of a biomolecule is a factor that favours the partition equilibrium displacement to the PEG-rich phase [23].…”

Partitioning features of bovine trypsin and α-chymotrypsin in polyethyleneglycol-sodium citrate aqueous two-phase systems

“…However, an anomalous behaviour -which cannot be only explained on the basis of the Albertsson electrostatic contribution -is observed for ATPSs formed by PEGs of low molecular weights. Protein partitioning behaviour showed to be sensitive to the surface hydrophobicity [13,14]. A high hydrophobical character of a biomolecule is a factor that favours the partition equilibrium displacement to the PEG-riched phase [15].…”

Measurement of the relative hydrophobicity of organic compounds without organic solvent. Effects of salt composition and pH on organic acids and nonionic compounds

“…It has been shown previously that correlations between the N(CH 2 ) and log D 7.40 values for three different series of drugs are described by three different parallel linear curves. 12 It seems reasonable to assume that either the resonance effects of nitro and methoxy groups on the properties of benzene ring 17 or speci®c interactions of these groups with octanol change the octanol±solute interactions for these compounds relative to those for other monosubstituted benzoic acids examined. This change would result in the partition behavior of nitro-and p-methoxybenzoic acids in an octanol±buffer system different from that typical for the other benzoic acids under study, and it would explain why these compounds appear to be outliers in the plot shown in Figure 6.…”