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Citation: LIU Yong-Ming, LI Gui-Zhi. Interaction of Enoxacin with Albumins by Fluorescence Quenching Analysis[J]. Chinese Journal of Applied Chemistry, ;2004, 21(6): 621-624. shu

Interaction of Enoxacin with Albumins by Fluorescence Quenching Analysis

LIU Yong-Ming ^, ,
LI Gui-Zhi

1.
College of Chemistry, Yantai University, Shangdong 264005

Corresponding author: LIU Yong-Ming,
Received Date: 29 July 2003
Available Online: 5 September 2003

The binding reactions of enoxacin with bovine serum albumin(BSA) or chicken egg albumin(CEA) in aqueous solution were studied by fluorescence and UV-Vis absorption spectrometry. The results indicated that enoxacin could bind with BSA or CEA strongly at molar ratio 1:1 and the equilibrium constants were K_BSA=8.02×10⁴ L/mol and K_CEA=4.51×10⁴ L/mol, respectively. The action distances(r_BSA=2.52 nm, r_CEA=2.74 nm) and energy transfer efficiencies(E_BSA=0.54, E_CEA=0.52) between donor(BSA,CEA) and acceptor(enoxacin) were calculated according to F9 rster's nonradiative energy transfer mechanism. Good linear Stern-Volmer lines were observed on the fluorescence of BSA or CEA quenched by enoxacin of different concentration, indicating the combination reaction of enoxacin with BSA or CEA is a single static quenching process.
- enoxacin,
- bovine serum albumin,
- chicken egg albumin,
- fluorescence quenching
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