Investigation of the Binding of Ginsenosides and Lysozyme by Electrospray Ionization Mass Spectrometry

• 来源期刊: 中国化学（英文版）
• 年，卷（期）: 2008,（11）
• 页码范围: 2073-2080
• 页数: 8页
• 语种: 英文

摘要

The noncovalent bindings of iysozyme(Ly)and ginsenoside Rg1 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 dissociation constant KD,1 values of lysozyme with Rgl or Re in different systems were consistent,but the KD,2 values were not.It can be concluded that the stronger the peak of the complex,the better the precision.Dissociation constants in-crease slightly with the increase of concentration of ginsenoside when the concentration of lysozyme is constant.However,dissociation constants decrease with the increase of concentration of lysozyme when the concentration of ginsenoside is constant.The experimental results also indicate that ginsenside Rg1 has higher affinity to lysozyme than ginsenoside Re.