Studies on the Interaction between Puerarin and Bovine Serum Albumin
ZHANG Guo-wen1,2,QUE Qing-min2, PAN Jun-hui2
1. The Key Laboratory of Food Science of Ministry of Education, Nanchang University, Nanchang 330047, China 2.Department of Food Science and Engineering, Nanchang University, Nanchang 330047, China
Abstract：The interaction of puerarin and bovine serum albumin(BSA) under physiological condition was studied by fluorospectrophotometry. The experiment demonstrated that the quenching mechanism of puerarin a BSA was static quenching process. The quenching constant is 7.29×1012 L·mol -1·s-1, and the binding constant is 5.04×104 L·mol-1. According to the Frster nonradiative energy transfer theory, the binding distance between donor (BSA) and acceptor (puerarin) was calculated to be 3.35 nm. The influence of the presence of puerarin on structure of BSA was studied by synochronous fluorescence method, the binding distance between BSA and puerarin was also measured, and the binding mechanism was discussed. In addition, the effect of some ions on the binding constant of puerarin with BSA was also studied.
张国文1,2,阙青民2,潘军辉2 . 葛根素与牛血清白蛋白相互作用的研究[J]. 光谱学与光谱分析, 2007, 27(09): 1784-1787.
ZHANG Guo-wen1,2,QUE Qing-min2, PAN Jun-hui2. Studies on the Interaction between Puerarin and Bovine Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(09): 1784-1787.
