芦丁与牛血清蛋白在不同条件下的相互作用研究

Study on the interaction between rutin andbovine serum albumin under different conditions

摘要: 依据芦丁对牛血清蛋白(BSA)的内源荧光的猝灭作用,采用荧光猝灭法研究了芦丁与血清白蛋白在不同条件下的相互作用.结果表明,芦丁与BSA之间主要因静电相互作用而发生结合反应,这一结合反应导致了蛋白质的荧光发生了猝灭,但并没有引起BSA的构象发生明显改变.芦丁与BSA的结合反应常数受介质pH、离子强度和金属离子种类影响明显.该结合常数在介质pH为8.0时具有最大值,但随离子强度的增加而减小,因Cu2+、Zn2+、Co2+、Fe2+、Mn2+的存在而增加.

Abstract: The interaction between rutin and bovine serum albumin (BSA) under the different conditions was studied using the fluorescence quenching method.The results indicated that the binding reaction between rutin and BSA through electrostatic forces was the main reasons for the fluorescence quenching phenomenon of BSA by rutin,but it almost did not affect the conformation of serum protein.Moreover,the binding constant of BSA to rutin was influenced by pH,ionic strength and the presence of various metal ions.The maximum binding constant was obtained at pH 8.0, but it increased with the decreasing of the ionic strength and it increased in the presence of Cu2+,Zn2+,Co2+,Fe2+ and Mn2+.