Fluorescence Study on the Interaction of Alizarin Yellow R and Bovine Serum Albumin in Alkali Solution
ZHANG Huan1, WANG Xing-ming1*, WANG Qing-cheng1, SHI Rong-ming1, DING Li-sheng2
1. Institute of Chemistry，Southwest University of Science and Technology, Mianyang 621010, China 2. Chengdu Institute of Biology， Chinese Academy of Sciences， Chengdu 610041, China
Abstract：The interaction of alizarin yellow R(AYR) and bovine serum albumin (BSA)was investigated by fluorescence method in alkali buffer solution. It was shown that AYR had a powerful ability to quench the BSA fluorescence at excitation and emission wavelengths of λex=393 nm and λem=641 nm in the medium solution of pH 11.00, and there were five binding sites of AYR to BSA;The combination reaction of AYR with BSA was a static quenching process, and from the effects of temperature on the fluorescence quenching rate of AYR-BSA and the Stern-Volmer quenching constant (KSV) and the Lineweaver-Burk quenching constant (KLB), the binding constant was calculated to be K=1.6×104 L·mol-1;as the enthalpy change ΔHθ＜0 and entropy change ΔSθ＜0, and AYR has an ability to quench the BSA-CBBG fluorescence, it can be deduced that the Van der Walls force and hydrogen bond are the main binding forces between AYR and BSA.
张欢1,王兴明1*,王清成1,石荣铭1,丁立生2 . 碱性介质中茜素黄R与牛血清白蛋白作用的荧光法研究[J]. 光谱学与光谱分析, 2006, 26(08): 1508-1512.
ZHANG Huan1, WANG Xing-ming1*, WANG Qing-cheng1, SHI Rong-ming1, DING Li-sheng2 . Fluorescence Study on the Interaction of Alizarin Yellow R and Bovine Serum Albumin in Alkali Solution. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(08): 1508-1512.
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