CONFORMATIONAL-CHANGES OF BOVINE SERUM-ALBUMIN UPON ITS ADSORPTION IN DODECANE-IN-WATER EMULSIONS AS REVEALED BY FRONT-FACE STEADY-STATE FLUORESCENCE

被引:53
作者
CASTELAIN, C
GENOT, C
机构
[1] Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, F-44026 Nantes Cédex 06
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 1994年 / 1199卷 / 01期
关键词
FRONT-FACE FLUORESCENCE; OIL-IN-WATER EMULSION; BOVINE SERUM ALBUMIN; ADSORPTION; PROTEIN CONFORMATION;
D O I
10.1016/0304-4165(94)90096-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Front-face fluorescence spectroscopy was used to characterise dodecane-in-buffer (0.1 M phosphate buffer, pH = 7.6) emulsions stabilised by bovine serum albumin (BSA). A 15-nm blue-shift of the emission maximum of the adsorbed protein and a significant increase of its fluorescence quantum yield were observed. The contribution of tyrosyl residues to total fluorescence was tentatilely evaluated from difference spectra and an R ratio taking into account the stray-light interference; R increased upon BSA adsorption but the Tyrosine contribution remained weak in all cases. Thus, conformational changes of the protein take place upon BSA adsorption onto the dodecane-water interface. They involve modifications in the environment of the protein aromatic amino acids especially of the tryptophanyl residues which are displaced to a more hydrophobic location. Moreover, the proportions of adsorbed and non-adsorbed BSA in emulsions can be estimated from the position of the emission maximum.
引用
收藏
页码:59 / 64
页数:6
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