【作者】 闫海刚；

【导师】 梁宏；

【作者基本信息】 广西师范大学 ， 无机化学， 2002， 硕士

【摘要】 第一部分：用平衡透析法，研究了生理pH(7.43)条件下Mn(Ⅱ)和Zn(Ⅱ)与牛血清白蛋白(bovine serum albumin，简称BSA)或人血清白蛋白(human serum albumin，简称HSA)的竞争结合平衡。通过三种不同的加入顺序，全面分析了Mn(Ⅱ)和Zn(Ⅱ)与血清白蛋白的竞争结合情况，并与它们的单金属体系作了比较。用非线性最小二乘法拟合Bjerrum方程，计算了同时竞争体系的逐级稳定常数；Scatchard图分析表明，三元体系中，Mn(Ⅱ)和Zn(Ⅱ)与血清白蛋白结强合部位数分别为2和1，与二元体系相比，保持不变，弱结合部位数随加入顺序的不同而不同，但都有所增加，竞争结果说明了Mn(Ⅱ)和Zn(Ⅱ)与血清白蛋白结合没有共同的强结合部位，强结合部位具有专一性，选择性，而弱结合部位具有不可逆性。竞争结果进一步表明了Mn(Ⅱ)和Zn(Ⅱ)之间具有明显的正协同效应，Hill图分析及自由能偶合定量分析也证明了此结论。 第二部分：本文应用荧光光谱法和共振散射光谱法，研究了生理pH(7.43)，等电点pH(5.4)条件下，银纳米粒子与血清白蛋白的结合，发现在低浓度比时有荧光增强效应(黄色银纳米粒子/BSA＜1，绿色银纳米粒子/BSA＜0.1)，较高浓度比范围时，则开始猝灭，银纳米粒子粒径越大，猝灭越明显，共振散射则有增强效应，讨论了二者之间的结合主要是利用静电力吸附。分析了荧光增强及猝灭机理，计算了猝灭常数。更多还原

【Abstract】 PartiThe cometition binding equilibrium of Mn (Ⅱ),Zn (Ⅱ) inos with HSA or BSAis studied by the method of equilibrium dialysis at physiological pH(7.43).The states of competition binding between Mn (Ⅱ),Zn (Ⅱ) and HSA or BSA were comprehensively analysised by three different addition sequence,the similarity and difference were compared with there single metal systems . The successive stability constants which are obtained by non-linear least-squares methord fitting Bjerrum formula. In three- system ,the results from Scatchard plots indicate that there exists two strong binding site of Mn (Ⅱ) and one strong binding site of Zn (Ⅱ),there are same results compareing with two -system ,but some more weak binding sites are different from the different addition sequence ,show that there are not common strong binding site of Mn (Ⅱ),Zn (Ⅱ) in HSA or BSA .Strong binding sites have electiveness and unfalteringness ,weak binding sites exists irreversibility.Competion results show that there exists clear positive cooperative effect between Mn (Ⅱ) and Zn (Ⅱ) binding with HSA or BSA,The analysis of Hill plots and free energy coupling support this conclusions.Part 2The interaction of serum albumin with Silver Nanoparticles has been studied by the fluorescence spectra and the resonance scattering spectra ,the enhancement of fluorescence occurs when concentration ratio of silver nonoparticles and serum albumin is low ( yellow[Ag] [BSA]<1,green[Agj [BSA]<0.1 ),the quenching occurs when concentration ratio is high. More big Particle diameter is ,more obvious the quenching of fiuorence is,the resonance scattering is more and more stronger with proportionate increasing. Adsorption between silver nonoparticles and serum albumin shows that serum albumin binds to silver nonoparticles mainly by electrostatic force.The mechanism of the fluorescence enhancement and quenching are analysised ,the quenching constants are calculated,,更多还原