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Improvement of the acridine orange–protein–surfactant system for protein estimation based on aromatic ring stacking effect of sodium dodecyl benzene sulphonate
Author(s) -
wang Fei,
Yang Jinghe,
Wu Xia,
Wang Xiaobo,
Guo Changying,
Jia Zhen
Publication year - 2006
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.904
Subject(s) - acridine orange , chemistry , bovine serum albumin , fluorescence , sodium dodecyl sulfate , chromatography , pulmonary surfactant , human serum albumin , benzene , stacking , acridine , sodium , biochemistry , organic chemistry , apoptosis , physics , quantum mechanics
Abstract The fluorescence of acridine orange (AO) is greatly quenched by the anionic surfactant sodium dodecyl benzene sulphonate (SDBS), but when protein is added into the AO–SDBS system, the fluorescence intensity of the latter is enhanced again. Based on this, a new fluorimetric method of determination of protein was developed. Under optimum conditions, the enhanced intensity of fluorescence is in proportion to the concentration of protein, such as bovine serum albumin (BSA), human serum albumin (HSA) and egg albumin (EA), over a wide range with detection limits at the 10 −9 g/mL level. This method has been satisfactorily used for the determination of protein in samples. We compared results using 280 nm and 490 nm excitation wavelengths and the mechanism of the assay. Copyright © 2006 John Wiley & Sons, Ltd.

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