Abstract

Studies on the Interaction of Florfenicol with Bovine Serum Albumin by Fluorescence and Synchronous Fluorescence Spectroscopy.

Author(s): Mengmeng Cui, Baosheng Liu, Tongtong Li and Shaotong Duan

By fluorescence and synchronous fluorescence spectroscopy, the interaction mechanism between florfenicol and bovine serum albumin was investigated at different temperatures. These two methods indicated that florfenicol could lead to flurescence quenching of bovine serum albumin. The process of fluorescence quenching was called static quenching. Electrostatic force bound florfenicol and bovine serum albumin. The order of magnitude about binding constant was up to 104. Binding site was approximately 1. The same conclusion could be obtained from these two different fluorescence spectroscopies.