Investigation of the interactions of quercetin and morin with trypsin.
The interactions of quercetin and morin with trypsin were investigated by UV-vis absorption, fluorescence, synchronous fluorescence and three-dimensional fluorescence spectra techniques under physiological pH 7.40. Quercetin and morin effectively quenched the intrinsic fluorescence of trypsin via static quenching. The process of binding quercetin and morin on trypsin was a spontaneous molecular interaction procedure. The binding constants and thermodynamic parameters at two different temperatures, the binding locality and the binding power were obtained. The conformation of trypsin was discussed by synchronous and three-dimensional fluorescence techniques.
Zhang
Hong-Mei
HM
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province 224002, People's Republic of China.
Wang
Yan-Qing
YQ
Zhou
Qiu-Hua
QH
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005419:Flavonoids / Q000378:metabolism*; D005453:Fluorescence; D011485:Protein Binding; D011794:Quercetin / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism*; D047309:Flavones
D005419:Flavonoids; D011794:Quercetin; D014357:Trypsin; C008548:morin; D047309:Flavones