The interaction of zincon (ZCN) with bovine serum albumin (BSA) and the cha
nges of its spectrum were studied by UV spectra at pH 4. 1 buffer solution.
The conditional constants, apparent molar absorptivity epsilon(p) = 1. 3 X
10(6) L . mol(-1) . cm(-1), maximum binding number n = 278 and apparent bi
nding equilibrium constant K-c = 8 X 10(7) were obtained, It was considered
that electrostatic force is the main binding force. The ion(sodium chlorid
e) concentration of the solution has significant effect on binding reaction
of BSA and ZCN, The effects of different denaturants were also examined. T
he Scatchard model is appropriate in the treatment of data, obtained.