Thermochemical Studies on the Reaction of Barbital Sodium with Bovine Serum Albumin
LIN Juan1,ZHAO Wei1,DING Fei1,JIANG Zhi-qiang2
1. School of Chemical Engineering and Technology,China University of Mining and Technology,Xuzhou 221008,China 2. College of Biology and Chemical Engineering,Panzhihua University,Panzhihua 617000,China
Abstract：The mechanism of interaction mechanism of barbital sodium with bovine serum albumin(BSA) was studied by fluorescence spectroscopy. According to the thermodynamics parameters,the main sort of binding force of the interaction is electrostatic force,and binding BBTS to BSA is a spontaneous supermolecular interaction in which entropy increases and Gibbs free energy decrease. The formation constants of them were analyzed according to Stern-Volmer equation and double-reciprocal equation,and are smaller at high temperature than at low temperature. It is confirmed that the combination reaction of BBTS with BSA is a static quenching process. The change in the micro-circumstance of amino of bovine serum albumin was analyzed by synchronous fluorescence spectrometry.
林娟1,赵炜1,丁飞1,蒋志强2. 巴比妥钠与牛血清白蛋白结合反应的热力学研究[J]. 光谱学与光谱分析, 2008, 28(03): 648-651.
LIN Juan1,ZHAO Wei1,DING Fei1,JIANG Zhi-qiang2. Thermochemical Studies on the Reaction of Barbital Sodium with Bovine Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2008, 28(03): 648-651.
