On the Interaction Between 2,4-Dichlorophenoxyacetic Acid and Bovine Serum Albumin

Mechanism of the interaction between 2,4-dichlorophenoxyacetic acid and bovine serum albumin (BSA) was studied by fluorospectrometry,UV-VIS spectrophotometry and circular dichroism spectrometry.It was found that fluorescence quenching of the interaction was due to static quenching.The binding constants,number of binding sites and types of binding force were found by applying the equation of site-binding model and thermodynamic equations.Circular dichroism spectrometry was used in the study of the effect of 2,4-dichlorophenoxyacetic acid on the configuration of BSA.