| Study on the interaction mechanism of lysozyme and bromophenol blue by fluorescence spectroscopy. | |
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MedLine Citation:
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PMID: 17682927 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The interaction of lysozyme with bromophenol blue (BPB) in acetate buffer (pH 6.0) was studied by fluorescence quenching method for the first time. It was found that BPB could conspicuously quench the fluorescence of lysozyme by the static quenching process, possibly due to the binding on the active site near Trp62. The binding parameters including the binding constant and the number of binding site were calculated. The thermodynamic parameters DeltaH degrees, DeltaS degrees and DeltaG degrees at different temperatures were obtained. The formation of lysozyme-BPB complex depended on the cooperation of the hydrophobic and electrostatic forces. And the binding average distance between lysozyme and BPB was determined. The effect of common metal ions on the binding constant of lysozyme-BPB was also examined. |
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Authors:
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Qiaoli Yue; Lichuan Niu; Xin Li; Xiaodong Shao; Xiaofeng Xie; Zhenghua Song |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2007-08-08 |
Journal Detail:
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Title: Journal of fluorescence Volume: 18 ISSN: 1053-0509 ISO Abbreviation: J Fluoresc Publication Date: 2008 Jan |
Date Detail:
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Created Date: 2008-01-14 Completed Date: 2008-05-05 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9201341 Medline TA: J Fluoresc Country: United States |
Other Details:
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Languages: eng Pagination: 11-5 Citation Subset: IM |
Affiliation:
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Department of Chemistry, Northwest University, Xi'an, 710069 China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bromphenol Blue
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metabolism* Energy Transfer Muramidase / metabolism* Protein Binding Spectrometry, Fluorescence* Thermodynamics |
| Chemical | |
Reg. No./Substance:
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115-39-9/Bromphenol Blue; EC 3.2.1.17/Muramidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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