CAJ | 학술논문

采用亲和毛细管电泳法,研究了牛血清蛋白（BSA）与两种结构相似的羧酸类化合物肉桂酸（CA）和阿魏酸（FA）间的相互作用。采用淌度比计算得到25℃时CA与FA的结合常数分别为3.5318×104L/mol、8.0158×104L/mol,并根据不同温度的结合常数计算了ΔS、ΔH、ΔG等热力学参数。热力学参数表明,CA、FA与BSA体系间的相互作用力以氢键作用力和范德华作用力为主。
채용친화모세관전영법,연구료우혈청단백（BSA）여량충결구상사적최산류화합물육계산（CA）화아위산（FA）간적상호작용。채용창도비계산득도25℃시CA여FA적결합상수분별위3.5318×104L/mol、8.0158×104L/mol,병근거불동온도적결합상수계산료ΔS、ΔH、ΔG등열역학삼수。열역학삼수표명,CA、FA여BSA체계간적상호작용력이경건작용력화범덕화작용력위주。
The interactions of bovine serum albumin(BSA) with cinnamic acid(CA) and ferulic acid(FA) were simultaneous studied by capillary electrophoresis(CE).Mobility ratio was used to deduce the binding constant(Kb).The Kb was 3.5318×104 L/mol and 8.0158×104 L/mol at 25 ℃ for CA and FA.The thermodynamic parameters were obtained from data at different temperatures,and the negative ΔH and positive ΔS values showed that both hydrogen bonds and van der Waals interactions played major roles in the binding of aromatic acids to BSA.