Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins.
The fluorescence method of Sklar et al. (Sklar, L.A., Hudson, B.S. and Simoni, R.D. (1977) Biochemistry 16, 5100-5108) using cis-parinaric acid as a probe was applied to determine the effective hydrophobicity of proteins. The initial slope (S0) of fluorescence intensity vs. protein concentration plot was used as an index of the protein hydrophobicity. A good correlation was observed for S0 of native proteins, denatured proteins and surfactant-bound proteins with an effective hydrophobicity determined by the hydrophobic partition method. The effective hydrophobicity determined fluorometrically showed significant correlations with interfacial tension and emulsifying activity of the proteins studied. The fluorescence technique using cis-parinaric acid is useful for determination of the effective hydrophobicity, as the procedure is much simpler and quicker than hydrophobic chromatography and hydrophobic partition.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004735:Energy Transfer; D005231:Fatty Acids, Unsaturated; D005456:Fluorescent Dyes; D011489:Protein Denaturation; D011506:Proteins; D013050:Spectrometry, Fluorescence / Q000379:methods; D013499:Surface Properties; D013500:Surface Tension; D014364:Tryptophan / Q000032:analysis
D005231:Fatty Acids, Unsaturated; D005456:Fluorescent Dyes; D011506:Proteins; D014364:Tryptophan; C013641:parinaric acid