光谱学与光谱分析 |
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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 |
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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.
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Received: 2005-11-01
Accepted: 2006-02-09
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Corresponding Authors:
WANG Xing-ming
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Cite this article: |
ZHANG Huan,WANG Xing-ming,WANG Qing-cheng, et al. Fluorescence Study on the Interaction of Alizarin Yellow R and Bovine Serum Albumin in Alkali Solution[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(08): 1508-1512.
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https://www.gpxygpfx.com/EN/Y2006/V26/I08/1508 |
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