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 Sterin-Volmer equation, Lineweaver-Burk equation and thermodynamic equation at 298. 15 K, the binding constant(K-LB = 3.601 X 10(5) L (.) mol(-1)) and thermodynamic parameters (Delta H-theta: - 22-66 kJ (.) mol(-1), Delta G(theta): -31. 30 kJ (.) mol(-1) and Delta S-theta: 36-32 J (.) 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.