Dissertation
Dissertation > Biological Sciences > Biochemistry > Material and energy metabolism

Binding Equilibrium Study between Ag(Ⅰ)、Au(Ⅲ) and Serum Albumin, Study on the Interaction of BSA with Cu(Ⅱ) and Zn(Ⅱ)

Author Song
Tutor LiangHong
School Guangxi Normal University
Course Organic Chemistry
Keywords Ag(Ⅰ) Au (Ⅲ) Cu(Ⅱ) and Zn(Ⅱ) Serum albumin Equilibrium dialysis Hysteretic effect UV-Visible spectrometry Resonance light-scatteringspectrum(RLS) Flurescence quenching
CLC Q591
Type Master's thesis
Year 2002
Downloads 242
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Part IThis paper has minutely studied the interaction between Ag( I ) and serum albumin.The binding of Ag( I ) to human serum albumin (HSA)or bovine serum albumin (BSA) has been studied by equilibrium dialysis at pH(5.4).The Scatchard analysis indicates that there exists several strong binding sites of Ag( I) in both HSA and BSA.A notable hysteretic effect has been observed In the interaction of Ag( I) with HSA or BSA using UV-Visible spectrometry at pH(5.4),which shows that the binding between Ag( I ) with HSA or BSA may induce a slow transition of HSA or BSA from the conformation of weaker affinity for Ag( I) to one of stronger affinity (A-B transition).The rate constants and activation parameters of this transition parameters of this tansition were measured and discussed.The binding equilibrium has been also studied by resonance light-scattering spectrum(RLS) and flurescence quenching.Part IIThis paper has minutely studied the interaction between Au (III) and serum albumin.The binding of Au (III) to human serum albumin (HSA)or bovine serum albumin (BSA) has been studied by equilibrium dialysis at pH(7.43 + 0.02).The Scatchard analysis indicates that there exists several strong binding sites of Au (III) in both HSA and BSA.A notable hysteretic effect has been observed in the interaction of Au (III) with HSA or BSA using UV-Visible spectrometry at pH(7.43 + 0.02),which shows that the binding between Au (III) with HSA or BSA may induce a slow transition of HSA or BSA from the conformation of weaker affinity for Au (III)to one of stronger affinity (A-B transition).The rate constants and activation parameters of this transition parameters of this tansition were measured and discussed.The binding equilibrium has Project supported by the National Science Foundation of China(NO.299621001),and the foundation for Talents of the ten hunred thousand in Guangxi.been also studied by flurescence quenching.Part IIIThe medicines about gold will be very popular in the next ten years. 25 ,physiologically pH 7.43(+0.02),applying resonance light-scattering spectrum(RLS),we observed the resonance light-scattering spectrum quenching of serum albumin by its interaction with Au(III) .A scattering peak at 350nm and its double frequency scattering peak at 700nm were observed when the excited wavelenth is 290nm. Their behaviour is similar as the resonance light-scattering. The intensities of Peak at about 350nm and 700nm decreased greatly after increasing the concentration of Au (III) .The reason of this phenomenon has been discussed in this paper.Part IVIn this paper,28 physiologically pH7.43(+0.02),applying fluorescence method,we observed the Fluorescece quenching of bovine serum albumin (BSA) by its interaction with Cu(II) and Zn(II) or Cu(II) absolutely.We calculated Stern-Volmer’s -K’svotBSA,and Lineweaver-Burk’s A^’DCU-BSA in these two kinds of systems.The different interaction of Cu( II) and Zn( II) with BSA has been discussed in this paper.

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