[Fluorescence quench of bovine serum albumin by pentachlorophenol].
The interaction between pentachlorophenol and bovine serum albumin (BSA) were studied using fluorescence spectra and ultraviolet-visible light absorption spectra. The results show that the fluorescence of BSA was quenched regularly by the pentachlorophenol, the mechanism of the fluorescence quench was investigated. The binding constants and thermodynamic parameters of pentachlorophenol with BSA were obtained at different temperatures. The hydrophobic interaction force and electrostatic force played a main role in the binding of pentachlorophenol with BSA. The distances of binding site between pentachlorophenol and BSA were also obtained according to the theory of Forster's non-radiative energy transfer.
Yu
Bing-chuan
BC
College of Resources and Environmental Sciences, Wuhan University, Wuhan 430072, China. yubc@163.com
Wu
Hong-te
HT
Zhou
Pei-jiang
PJ
Nan
Shu-qing
SQ
Lu
Guang-han
GH
Song
Feng
F
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D010416:Pentachlorophenol / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D012710:Serum Albumin, Bovine; D010416:Pentachlorophenol