作者: Zhi-Ping Cui , Shao-Pu Liu , Zhong-Fang Liu , Hu-Zhi Zheng , Xiao-Li Hu
DOI: 10.1002/BIO.2614
关键词: Resonance 、 Human serum albumin 、 Circular dichroism 、 Ion 、 Absorption spectroscopy 、 Rayleigh scattering 、 Chemistry 、 Scattering 、 Analytical chemistry 、 Bovine serum albumin
摘要: In weak acid medium, aluminum(III) can react with chlorophosphonazo III [CPA(III), H8L] to form a 1:1 coordination anion [Al(OH)(H4L)]2-. At the same time, proteins such as bovine serum albumin (BSA), lysozyme (Lyso) and human (HSA) existed large cations positive charges, which further combined [Al(OH)(H4L)]2- 1:4 chelate. This resulted in significant enhancement of resonance Rayleigh scattering (RRS), second-order (SOS) frequency doubling (FDS). this study, we investigated interaction between proteins, optimization reaction conditions spectral characteristics RRS, SOS FDS. The maximum RRS wavelengths different protein systems were located at 357–370 nm. FDS 546 389 nm, respectively. intensities (ΔI) three methods proportional concentration within certain ranges, detection limits most sensitive method 2.6–9.3 ng/mL. Moreover, chelate mechanism or reasons for discussed through absorption spectra, fluorescence spectra circular dichroism (CD) spectra. Copyright © 2013 John Wiley & Sons, Ltd.