摘要
分别研究了21℃和29℃时,磺胺噻唑与牛血清白蛋白作用的荧光猝灭光谱和同步荧光光谱特征.求出这两个温度下的猝灭常数,推断出磺胺噻唑与牛血清白蛋白间的相互作用是以动态猝灭为主的猝灭过程.根据F rster非辐射能量转移理论,计算出磺胺噻唑在蛋白质中的结合位置与212位色氨酸残基间的距离为4.163 nm,并求得21℃的结合常数和结合位点数分别为4.335×105L.mol-1和1.217.由求得的热力学参数,证实了磺胺噻唑与牛血清白蛋白之间主要通过疏水作用力结合.用同步荧光光谱技术探讨了磺胺噻唑对牛血清白蛋白构象的影响,考察了Ca2+、Mg2+、Zn2+或Cu2+对磺胺噻唑与牛血清蛋白相互作用的影响.
The spectra characteristics of interaction between sulfathiazole （ST） and bovine serum albumin （BSA） was studied by fluorescence quenching and synchronous fluorescence techniques at 21℃ and 29℃. It was proved that mainly dynamic quenching exits between sulfonamides and BSA. Quenching constant was obtained at the two temperatures. The binding locality was an distance of 4. 163 nm away from tryptophan residue -212 in BSA based on Foerster＇ s non-radiation energy transfer mechanism. The binding constant is 4. 335 × 10^5 L· mol^-1 and the number of binding sites is 1. 217 at 21℃ respectively. According to the thermodynamic parameters, the binding power between ST and BSA is mainly the hydrophobic interaction. The effect of ST on the conformation of BSA was analyzed by synchronous spectra. In addition, the effect of Ca^2＋ ,Mg^2＋ ,Zn^2＋ and Cu^2＋ on the binding interaction between ST and BSA was also studied.
出处
《南昌大学学报（工科版）》
CAS
2007年第3期225-228,248,共5页
Journal of Nanchang University(Engineering & Technology)
基金
教育部长江学者和创新团队发展计划资助项目(IRT0540)
南昌大学博士科研基金启动项目
关键词
荧光光谱法
磺胺噻唑
牛血清白蛋白
相互作用
fluorescence spectrometry
sulfathiazole
bovine serum albumin
interaction
