[Studies on the features of binding reaction of eosin Y with bovine serum albumin].
The binding of eosin Y to bovine serum albumin (BSA) was studied by fluorescence spectroscopy and ultraviolet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence from BSA. After analyzing the fluorescence quenching data according to Sterm-Volmer equation, Lineweaver-Burk equation and thermodynamic equation at 298. 15 K, the binding constant(KLB= 3. 601 x 10(5) L x mol(-1)) and thermodynamic parameters (deltaHtheta: - 22. 66 kJ x mol(-1), deltaGtheta: -31. 30 kJ x mol(-1) and deltaStheta: 36.32 J x K(-1)were obtained, which provide important information for researching the configuration modification of BSA caused by added eosin Y, biological effects of eosin Y in a living body, and dyeing mechanism of cells.
Yan
Cheng-nong
CN
College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou 434020, China.
Mei
Ping
P
Xiong
Dan
D
Liu
Yi
Y
D000818:Animals; D002417:Cattle; D004801:Eosine Yellowish-(YS) / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D004801:Eosine Yellowish-(YS)