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Investigation of the Binding of Ginsenosides and Lysozyme by Electrospray Ionization Mass Spectrometry
Author(s) -
QU ChenLing,
DING Lan,
ZHANG HuaRong,
WANG YuTang,
BAI YuPing,
ZHANG HanQi
Publication year - 2008
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200890370
Subject(s) - chemistry , lysozyme , electrospray ionization , mass spectrometry , dissociation constant , electrospray , ionization , ginsenoside , dissociation (chemistry) , chromatography , analytical chemistry (journal) , computational chemistry , ion , ginseng , organic chemistry , biochemistry , medicine , receptor , alternative medicine , pathology
The noncovalent bindings of lysozyme (Ly) and ginsenoside Rg 1 or Re were studied by electrospray ionization mass spectrometry. The dissociation constants of the noncovalent complexes were directly calculated based on the peak intensities of the lysozyme and the complexes of lysozyme and ginsenoside in mass spectra. The experimental results also indicate that ginsenside Rg 1 has higher affinity to lysozyme than ginsenoside Re. It is obvious that the direct calculating method, which based on the mass spectrometry peak intensity and applied to work out the dissociation constant in this investigation without curve fitting, can simplify calculation. Therefore, this direct calculating method can be extensively applied to obtain the dissociation constants for other interactions.