Fluorescence quenching study of quercetin interaction with bovine milk xanthine oxidase
| Autor: | Abdolhossein Naseri, Hamideh Nadjarpour Jabary, Farzaneh Rasoulzadeh, Mohammad-Reza Rashidi |
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| Rok vydání: | 2009 |
| Předmět: |
Xanthine Oxidase
Stereochemistry medicine.drug_class Flavonoid Allopurinol Analytical Chemistry chemistry.chemical_compound medicine Animals Xanthine oxidase Instrumentation Xanthine oxidase inhibitor Spectroscopy chemistry.chemical_classification Binding Sites Chemistry food and beverages Binding constant Combinatorial chemistry Atomic and Molecular Physics and Optics Kinetics Milk Spectrometry Fluorescence Enzyme Polyphenol Thermodynamics Cattle Quercetin medicine.drug |
| Zdroj: | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 72:190-193 |
| ISSN: | 1386-1425 |
| Popis: | Quercetin is a natural flavonoid with many important therapeutic properties. The interaction of this polyphenolic compound bovine milk xanthine oxidase as one of its major target proteins was studied using fluorescence quenching method for the first time. It was found that the fluorescence quenching of xanthine oxidase occurs through a static mechanism. The results revealed the presence of a single binding site on xanthine oxidase with the binding constant value equals to 1.153 × 10 4 l mol −1 at 310 K and pH 7.4. The thermodynamic parameters were also calculated at different temperatures. The enthalpy and entropy changes were found as −10.661 kJ mol −1 and +43.321 J mol −1 K −1 indicating that both hydrogen binding and hydrophobic are involved in the interaction of this polyphenolic natural compound with xanthine oxidase. The results may provide a ground for further studies with different flavonoids to find a safe alternative for allopurinol, the only xanthine oxidase inhibitor with clinical application. |
| Databáze: | OpenAIRE |
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