| 光谱学与光谱分析 |
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| Reaction Mechanism of Cefotaxime with Human Serum Albumin |
| LIU Luo-sheng1, WANG Xing-po1, ZHAO Quan-qin1, ZHANG Yu-yi2 |
1. School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China
2. School of Medicine, Shandong University, Jinan 250012, China |
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Abstract The reaction mechanism of cefotaxime with human serum albumin (HSA) and the affinity between cefotaxime and β-lactamase were investigated by spectrometry and spectrofluorimetry. The interaction dissociation constants of human serum albumin and cefotaxime were determined from a double reciprocal Lineweaver-Burk plot. The binding distance and transfer efficiency between cefotaxime and HSA were also obtained according to the theory of Frster non-radiation energy transfer. The result suggested that the main binding force between cefotaxime and HSA is electrostatic force interaction. The high β-lactamase stability of cefotaxime may be correlative with its molecular structure. The antibiotic activity and valence are connected with transfer efficiency and dissociation constant. The effect of cefotaxime on the conformation of HSA was also analyzed using synchronous fluorescence spectrometry.
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Received: 2005-03-16
Accepted: 2005-10-06
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Corresponding Authors:
LIU Luo-sheng
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| Cite this article: |
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LIU Luo-sheng,WANG Xing-po,ZHAO Quan-qin, et al. Reaction Mechanism of Cefotaxime with Human Serum Albumin[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2006, 26(06): 1130-1133.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2006/V26/I06/1130 |
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