CAJ | 학술논문

在模拟生理条件下，用荧光光谱法研究了十六烷基三甲基溴化铵（ CTAB）与牛血清白蛋白（ BSA）的相互作用。结果表明：BSA分子中色氨酸和酪氨酸残基具有荧光发射性质，以280 nm激发BSA，在341 nm处有很强的荧光发射。在加入CTAB后，发现CTAB-BSA强荧光峰的位置蓝移，且荧光强度随着CTAB浓度的增大而明显减弱，说明CTAB对BSA 有荧光猝灭现象，猝灭以静态猝灭为主，由Stern-Volmer方程求得CTAB表观猝灭常数Kq ＝1.469×1013 L· mol-1· s-1。得到了CTAB与牛血清白蛋白分子间的结合常数和热力学参数。利用已有的计算方法，建立了相应的计算机程序，使计算结果更合理。通过与常见公式计算的结果进行比较，所建立的方法得到了比较满意的结果。
재모의생리조건하，용형광광보법연구료십륙완기삼갑기추화안（ CTAB）여우혈청백단백（ BSA）적상호작용。결과표명：BSA분자중색안산화락안산잔기구유형광발사성질，이280 nm격발BSA，재341 nm처유흔강적형광발사。재가입CTAB후，발현CTAB-BSA강형광봉적위치람이，차형광강도수착CTAB농도적증대이명현감약，설명CTAB대BSA 유형광졸멸현상，졸멸이정태졸멸위주，유Stern-Volmer방정구득CTAB표관졸멸상수Kq ＝1.469×1013 L· mol-1· s-1。득도료CTAB여우혈청백단백분자간적결합상수화열역학삼수。이용이유적계산방법，건립료상응적계산궤정서，사계산결과경합리。통과여상견공식계산적결과진행비교，소건립적방법득도료비교만의적결과。
The interaction of cetyltrimethylammonium bromide ( CTAB ) and bovine serum albumin ( BSA ) was studied under conditions similar to those in human bodies by fluorescence spectra.The results indicated that CTAB, which was located in BSA, had a max fluorescence emission peak at 341 nm with an excitation wavelength of 280 nm.It showed that CTAB had a powerful ability to quench the BSA fluorescence with a mechanism of a static process rather than a dynamic one.The apparent quenching constant Kq was obtained to be 1.469 ×1013 L· mol-1 · s-1 by Stern-Volmer equation.The binding and thermodynamic parameters were obtained.The reasonable results were obtained by programmed calculation process based on the calculating equation established.By comparison with the results obtained by other calculating methods, it was proved that the satisfactory results can be obtained by the proposed method.