CAJ | 학술논문

分别在298,310,318 K温度下,利用荧光光谱法研究了pH=7.40生理条件下硝基羟乙唑（ TRI）与溶菌酶（ LYSO）的相互作用机理。结果表明,TRI与LYSO间通过静态猝灭方式相互作用。测定了LYSO与TRI反应的结合常数、结合位点数。利用反应过程的热力学参数,确定了LYSO-TRI体系的作用力类型；由Hill系数得出了LYSO或TRI的协同性；根据非辐射能量转移理论,确定了TRI到LYSO的结合距离,同时采用同步光谱法考察了TRI对LYSO构象的影响。
분별재298,310,318 K온도하,이용형광광보법연구료pH=7.40생리조건하초기간을서（ TRI）여용균매（ LYSO）적상호작용궤리。결과표명,TRI여LYSO간통과정태졸멸방식상호작용。측정료LYSO여TRI반응적결합상수、결합위점수。이용반응과정적열역학삼수,학정료LYSO-TRI체계적작용력류형；유Hill계수득출료LYSO혹TRI적협동성；근거비복사능량전이이론,학정료TRI도LYSO적결합거리,동시채용동보광보법고찰료TRI대LYSO구상적영향。
The interaction mechanism of trichazol ( TRI) to lysozyme( LYSO) at different tempera-tures (298, 310, 318 K) was investigated using fluorescence spectroscopy under simulative physio-logical conditions. The results clearly demonstrated that TRI caused strong quenching of the fluores-cence of LYSO by a static quenching mechanism. The binding constants were order of magnitude of 104 and the number of binding site in the interaction was closed to 1. The thermodynamic parameters of LYSO-TRI system were determined as follows:negativeΔH and positiveΔS, which indicated that electrostatic interaction played a major role in the binding reaction. The effect of cooperative binding of TRI was quantified by Hill’s coefficient (nH) and the values of nH were slightly more than 1 in the systems, which indicated weakly positive cooperativeness in the interaction of TRI with LYSO. The binding distance ( r) between TRI and LYSO was obtained based on the F?rster nonradioactive reso-nance energy transfer and r was less than 7 nm. Furthermore, the effect of TRI on the conformation of LYSO was analyzed by using the synchronous fluorescence spectroscopy.