发光学报2011,Vol.32Issue(3):293-299,7.DOI:10.3788/fgxb20113203.0293
硫酸头孢匹罗与牛血清白蛋白结合反应的发光机理
Luminescence Mechanism Study of The Conjugation Reaction between Cefpirome Sulfate and Bovine Serum Albumin
摘要
Abstract
In human physical conditions, the binding reaction between cefpirome sulfate (CPS) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy and resonance light scattering (RLS) at different temperatures. Results showed that both fluorescence and RLS of BSA reduced with the increased concentration of CPS, and the effect between CPS and BSA was static fluorescence quenching process with F(0)rester spectroscopy energy transfer. The scope of apparent binding eonstants (Ka) was ~ 104; the corresponding binding site value (n) in the binary systems was 1; the binding distances (r) were much smaller than 7 nm and the primary binding site for CPS was located at site Ⅰ in subdomain Ⅱ A of BSA. Besides, the electrostatic attraction plays an important role in the conjugation reaction of BSA and CPS. The values of Hill's coefficients were less than 1, which indicated that there was some negative cooperative effect. Studies utilizing synchronous spectra showed that the conjugation reaction between CPS and BSA would affect the conformation of BSA, leading to the polarity around BSA strengthened and the hydrophobicity weakened.关键词
牛血清白蛋白/硫酸头孢匹罗/结合反应/发光机理Key words
bovine serum albumin/ cefpirome sulfate/ conjugation reaction/ luminescence mechanism分类
数理科学引用本文复制引用
刘保生,杨超,王晶,薛春丽,吕运开..硫酸头孢匹罗与牛血清白蛋白结合反应的发光机理[J].发光学报,2011,32(3):293-299,7.基金项目
国家自然科学基金(20675024) (20675024)
河北省重点基础研究项目(10967126D)资助 (10967126D)