CAJ | 학술논문

　　本研究采用紫外和荧光光谱分析法研究了生理pH条件下盐酸异丙肾上腺素（ HAI ）与牛血清白蛋白（BSA）在不同温度（25℃和37℃）下的相互作用。实验结果表明，HAI使BSA紫外吸收峰增强，并使BSA的特征荧光峰猝灭，表明HAI与BSA形成结合物。 HAI对BSA荧光猝灭机制为静态猝灭，属于单位点结合。25℃时两者之间的结合常数为7.41×103 L· mol-1，ΔG为-22.10 kJ· mol-1，ΔH为25.86 kJ· mol-1，ΔS为940 J· mol-1。37℃时的结合常数为4.26×105 L· mol-1，ΔH和ΔS与25℃时相同，ΔG为-33.41 kJ· mol-1。以上热力学参数表明HAI与BSA之间的结合属自发过程，两者之间的作用力以疏水作用为主。根据F迸ster非辐射能量转移理论计算出HAI与BSA间的结合距离为2.503 nm。
　　본연구채용자외화형광광보분석법연구료생리pH조건하염산이병신상선소（ HAI ）여우혈청백단백（BSA）재불동온도（25℃화37℃）하적상호작용。실험결과표명，HAI사BSA자외흡수봉증강，병사BSA적특정형광봉졸멸，표명HAI여BSA형성결합물。 HAI대BSA형광졸멸궤제위정태졸멸，속우단위점결합。25℃시량자지간적결합상수위7.41×103 L· mol-1，ΔG위-22.10 kJ· mol-1，ΔH위25.86 kJ· mol-1，ΔS위940 J· mol-1。37℃시적결합상수위4.26×105 L· mol-1，ΔH화ΔS여25℃시상동，ΔG위-33.41 kJ· mol-1。이상열역학삼수표명HAI여BSA지간적결합속자발과정，량자지간적작용력이소수작용위주。근거F병ster비복사능량전이이론계산출HAI여BSA간적결합거리위2.503 nm。
The interaction between Bovine Serum Albumin (BSA)and hydrochloric acid isoproterenol (HAI)was investigated by ul-traviolet and fluorescence spectroscopic methods.Ultraviolet of BSA is increasing with the increase of HAI content .It is proved that the fluorescence quenching of BSA by HAI is a result of the formation of BSA-HAI complex.The fluorescence quenching mechanism belongs to constant quenching.The number of interaction point between HAI and BSA is just one.The interacted constant of them was 7.41 ×10 3 L · mol-1 and 4.26 ×10 5 L · mol-1 at 25℃ and 37℃, respectively.Changes of Gibbs free energy (ΔG ) , Enthalpy (ΔH),and Entropy(ΔS)were-22.10kJ· mol-1,25.86 kJ· mol-1,and 940 J· mol-1,respectively at 25℃.Changes of Enthalpy and Entropy at 37℃were same with 25℃.While,theΔG was-33.41 kJ· mol-1 at 37℃.From thermodynamic coordination it can be jud-ges that the binding power between HAI and BSA is hydrophobic power.And the binding of HAI and BSA is a spontaneous process . According to the F?ster dipole-dipole energy transfer ,the distance between the HAI and tryptophane of BSA is 2.503 nm.