2009
DOI: 10.1016/j.saa.2008.09.021
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Fluorescence quenching study of quercetin interaction with bovine milk xanthine oxidase

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Cited by 90 publications
(39 citation statements)
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“…(6) and (7). (Li et al, 2007;Rasoulzadeh, Najarpour, Naseri, & Rashidi, 2009;Shohrati et al, 2007). The thermodynamic parameters for the interaction of quinoline yellow with BSA are shown in Table 1.…”
Section: Thermodynamic Parameters and Nature Of Binding Forcesmentioning
confidence: 99%
“…(6) and (7). (Li et al, 2007;Rasoulzadeh, Najarpour, Naseri, & Rashidi, 2009;Shohrati et al, 2007). The thermodynamic parameters for the interaction of quinoline yellow with BSA are shown in Table 1.…”
Section: Thermodynamic Parameters and Nature Of Binding Forcesmentioning
confidence: 99%
“…The maximum value possible for diffusion-limited quenching (dynamic mechanism) in water is 10 10 M À1 s À1 . When the bimolecular quenching constant is higher, a complex between protein and quencher is formed, corresponding to a static mechanism (Johansson, 1997;Rasoulzadeh, Jabary, Naseri, & Rashidi, 2009). The results obtained indicate that the mechanism by which these procyanidins fractions associate with a-amylase is of a static type involving a stable interaction between the two.…”
Section: Fluorescence Quenchingmentioning
confidence: 99%
“…By means of analysis of the fluorescence parameters, much information concerning the structural changes in biomacromolecules can be obtained [8].…”
Section: Introductionmentioning
confidence: 99%