Surface hydrophobicity of a low molecular weight basic trypsin subtilisin inhibitor from marine turtle eggwhite.

Surface hydrophobicity has recently been emphasized as an important parameter for functional correlation of proteins. However, evaluations of the parameter by different experimental techniques often do not correlate well with each other. In this paper we have compared surface hydrophobicity of a basic protein with those of beta-lactoglobulin, ovalbumin and lysozyme by fluorescence probe method using ANS as an external probe. Two different fluorimetric approaches to determining the surface hydrophobicity parameter, namely, the slope method and the binding parameter method, follow the same relative order. Denaturants, urea, and guanidine hydrochloride disrupted the hydrophobic clefts of the inhibitor on the surface, causing a drastic reduction of surface hydrophobicity.