[Mechanism studies on the combination reaction between bovine serum albumin and zincon by fluorescence spectra].
The characteristics of binding reaction between bovine serum albumin (BSA) and zincon (ZCN) were studied by fluorescence spectra and ultraviolet-visible absorption spectra. The bovine serum albumin can emit fluorescence (lamda(em) = 345 nm) under irradiation of ultraviolet light (lamda(ex) = 280 nm). After the zincon (ZCN) was added into BSA solution the fluorescence of BSA was quenched partially. The results indicated that ZCN was strongly bound to BSA. According to Stern-Volmer equation and Lineweaver-Burk equation, the quenching constant and the thermodynamic parameters were obtained. From the thermodynamic parameters the binding power between ZCN and BSA can be judged. The binding distance (r = 5.07 nm) and energy transfer efficiency (E = 0.67) between donor (BSA) and acceptor (ZCN) were obtained by Forster's non-radiative energy transfer mechanism. It is confirmed that the combination reaction between ZCN and BSA is a single static quenching process, and their interaction may be interpreted with energy transfer mechanism.
Jiang
Zhi-qiang
ZQ
Department of Chemistry, School of Materials Science and Engineering, Southwest University of Science and Technology, Mianyang 621010, China.
Chi
Yan-hua
YH
Zhuang
Jia
J
Bi
Xin-ying
XY
Zhou
Lei
L
D000818:Animals; D001391:Azo Compounds / Q000737:chemistry*; D002417:Cattle; D005562:Formazans; D012710:Serum Albumin, Bovine / Q000032:analysis* / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013053:Spectrophotometry; D013816:Thermodynamics
D001391:Azo Compounds; D005562:Formazans; D012710:Serum Albumin, Bovine; C009809:2-carboxy-2'-hydroxy-5'-sulfoformazylbenzene