2011
DOI: 10.1007/s00217-011-1491-z
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Probing the interaction between 3 flavonoids and pancreatic lipase by methods of fluorescence spectroscopy and enzymatic kinetics

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Cited by 56 publications
(59 citation statements)
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“…The 7 inhibition lines of PL intersect on the x-axis indicated that the mechanism of pancreatic lipase inhibition by WE, ME, EE, CE, NBE and EAE was noncompetitive type. This was similar to the result obtain by Li [3] but diametrically opposed to Martins [18]. The data showed that the extracts and substrate could bind to pancreatic lipase simultaneously.…”
Section: Kinetics Of Enzyme Inhibitionsupporting
confidence: 89%
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“…The 7 inhibition lines of PL intersect on the x-axis indicated that the mechanism of pancreatic lipase inhibition by WE, ME, EE, CE, NBE and EAE was noncompetitive type. This was similar to the result obtain by Li [3] but diametrically opposed to Martins [18]. The data showed that the extracts and substrate could bind to pancreatic lipase simultaneously.…”
Section: Kinetics Of Enzyme Inhibitionsupporting
confidence: 89%
“…When the concentration of orlistat > 400 μg/mL, the inhibition rate reaches 100%. Nevertheless, the extracts still showed a strong inhibitory activity of pancreatic lipase compared with quercetin, isoquercitrin and rutin [3], especially ME. To some extent, The IC 50 values showed the inhibitory effect of inhibitors on enzyme active under a particular substrate concentration.…”
Section: Pancreatic Lipase Inhibitory Activitymentioning
confidence: 88%
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“…Fluorescence spectroscopy is widely used to investigate the interaction between proteins and small molecule compounds [39]. When the excitation wavelength is set at 280 nm, the intrinsic fluorescence of protein at 340 nm is mainly contributed by tryptophan (Trp) and tyrosine (Tyr) residues.…”
Section: Fluorescence Quenching Of Lipase By the Inhibitorsmentioning
confidence: 99%