期刊
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
卷 36, 期 4, 页码 915-919出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jpba.2004.08.021
关键词
monoammonium glycyrrhizinate; bovine serum albumin; fluorescence quenching; UV-vis spectroscopy; thermodynamic parameters; energy transfer
The interaction between monoammonium glycyrrhizinate (MAG) and bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by monoammonium glycyrrhizinate was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters DeltaHdegrees, DeltaGdegrees, DeltaSdegrees at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (monoammonium glycyrrhizinate) was obtained according to Forster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed. (C) 2004 Elsevier B.V. All rights reserved.
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