Chin. J. Anal. Chem.

The binding of Triton X-100 (Tx) to bovine serum albumin(BSA) was studied using fluorescence spectroscopy. It was shown that TX has a strong ability to quench the BSA fluorescence mainly via a static quenching. The binding constant K and the number of bindig n were obtained from the fluorescence quenching results. It was revealed that K and n were changed with varying concentrations of TX: below cmc of TX, K was 440 mol/L, n was 0.91; above cmc, K was 10 mg/L, n was 0.42. The hydrophobic interactions played a major role in the binding process.The binding of Triton X-100 (Tx) to bovine serum albumin(BSA) was studied using fluorescence spectroscopy. It was shown that TX has a strong ability to quench the BSA fluorescence mainly via a static quenching. The binding constant K and the number of bindig n were obtained from the fluorescence quenching results. It was revealed that K and n were changed with varying concentrations of TX: below cmc of TX, K was 440 mol/L, n was 0.91; above cmc, K was 10 mg/L, n was 0.42. The hydrophobic interactions played a major role in the binding process