| 光谱学与光谱分析 |
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| Study on the Interaction of Methyl Pheophorbide-a and Bovine Serum Albumins by Fluorescence |
| LIU Yong-ming,WANG Jin-jun,WU Xu-ran |
| College of Chemistry, Yantai University, Yantai 264005, China |
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Abstract The binding reaction of methyl pheophorbide-a with bovine serum albumins (BSA) in aqueous solution was studied by fluorescence and UV-Vis absorption spectra. The results indicated that the combination reaction of them was a single static quenching process. In aqueous solution, methyl pheophorbide-a strongly bound BSA with the apparent molar ratio of 2∶1 because of methyl pheophorbide-a polymerized by itself. The binding constant KB was 6.7×104 L·mol-1. In mixture solvent of tetrahydrofuran and water, methyl pheophorbide-a existed as single molecule and bound BSA with a molar ratio of 1∶1. There is single position for combining methyl pheophorbide-a with BSA. The shortest binding distance (r=3.50 nm) and energy transfer efficiencies (E=0.39) between donor (BSA) and acceptor (methyl pheophorbide-a) were obtained by Frster′s nonradiative energy transfer mechanism.
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Received: 2003-12-18
Accepted: 2004-04-22
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Corresponding Authors:
LIU Yong-ming
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| Cite this article: |
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LIU Yong-ming,WANG Jin-jun,WU Xu-ran. Study on the Interaction of Methyl Pheophorbide-a and Bovine Serum Albumins by Fluorescence[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(05): 747-750.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2005/V25/I05/747 |
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