CAJ | 학술논문

在模拟人体生理条件下，应用荧光光谱法、紫外-可见光谱法研究了邻硝基酚（o-nitrophenol）与牛血清白蛋白（BSA）的相互作用。结果表明：邻硝基酚使BSA"源荧光猝灭的机制是其与BSA形成了基态复合物。用 van’t Hoff方程计算出的热力学参数焓变（ΔH）和熵变（ΔS）分别为19．09 KJ·mol-1和150．66 J·k-1·mol-1，说明维持邻硝基酚-BSA复合物稳定的作用力主要是疏水作用力。位点竞争实验的结果表明，邻硝基酚与 BSA的结合位点主要在BSA的亚域ⅡA上（siteI位），结合常数是3．35×104 L·mol-1，结合位点数是1．09。同步荧光光谱分析结果显示，邻硝基酚的存在使BSA构象只发生微弱改变。
재모의인체생리조건하，응용형광광보법、자외-가견광보법연구료린초기분（o-nitrophenol）여우혈청백단백（BSA）적상호작용。결과표명：린초기분사BSA"원형광졸멸적궤제시기여BSA형성료기태복합물。용 van’t Hoff방정계산출적열역학삼수함변（ΔH）화적변（ΔS）분별위19．09 KJ·mol-1화150．66 J·k-1·mol-1，설명유지린초기분-BSA복합물은정적작용력주요시소수작용력。위점경쟁실험적결과표명，린초기분여 BSA적결합위점주요재BSA적아역ⅡA상（siteI위），결합상수시3．35×104 L·mol-1，결합위점수시1．09。동보형광광보분석결과현시，린초기분적존재사BSA구상지발생미약개변。
The interactions between o-nitrophenol and bovine serum albumin(BSA)were investigated by fluorescence,UV-vis absorption spectroscopy under simulative physiological conditions (pH=7.4).Our re-sults suggested that the intrinsic fluorescence of BSA could be quenched by o-nitrophenol,which was prob-ably a result of the formation of o-nitrophenol-BSA complex.According to the van't Hoff equation,the thermodynamics parameters enthalpy change(ΔH)and entropy change(ΔS)were calculated to be 19.09 KJ ·mol-1 and 150.66 J·k-1 ·mol-1 ,respectively,which indicated that hydrophobic interaction was the pre-dominant intermolecular force in stabilizing the complex.The site marker competitive experiments also re-vealed that the binding of o-nitrophenol to BSA mainly took place in subdomainⅡA(siteI),the binding constant is 3.35×104 L·mol-1 ,and the number of binding sites is 1.09.The results of synchronous fluo-rescence indicated that o-nitrophenol had little influence on the conformation of BSA.