牛血清蛋白与6,6′-(3H-21-苯并噁硫醇-3-叉)二百里酚作用研究  

A Study on the Reaction of Bovine Serum Albumin with Thymol Blue

作　　者：王兴明[1] 董发勤[1] 丁立生[2] 

机构地区：[1]西南科技大学材料学院化学与生物工程系,四川绵阳621010 [2]中国科学院成都生物研究所,成都610041

出　　处：《化学通报》2005年第4期309-313,共5页Chemistry

基　　金：国家自然科学基金 (40 0 72 0 2 0 );四川省教育厅自然科学基金 (2 0 0 0_A5 6 )资助项目

摘　　要：应用UV-Vis光谱法 ,研究了在pH =1 . 61的酸性缓冲溶液中 ,牛血清蛋白 (BSA)与 6,6′-(3H-2 1-苯并硫醇-3-叉 )二百里酚 (TB)的相互作用。测得生成复合物的最大吸收峰为 440nm ,与试剂相比蓝移 1 0 5nm。微环境的影响使BSA-TB复合物的最大吸收波长之间红移约 3 0nm。应用平衡透析法、摩尔比法和双波长法进行测定 ,结果表明 ,表观摩尔吸光系数εB=1 . 40× 1 0 4L·mol-1·cm-1,平均结合数n =7,表观结合平衡常数K =2 . 5 9× 1 0 6。研究发现 ,该反应基本符合Scatchard模型 ,认为是BSA与TB之间以静电引力和疏水力综合作用的结果。The interaction of bovine serum albumin (BSA) an d thymol blue (TB) were investigated by spectrophotometric method in acidic cush ion solution(pH=1.61).When BSA was added into TB, a yellow color was observed,w hich indicated the formation of the BSA-TB complex compound. Its maxim um absorption of formative yellow color complex compound was at 440 nm. It was found that maximum absorption of the compound was shifted to 105nm. Microenvironment effect gave rise to the maximum absorption wavelengh shift a bout 30nm toward BSA_TB complex compounds. According to balance percolation met hod, molar ratio method and double wavelengh method,the apparent molar absorpti v ity of ε B=1.40×10 4 L·mol -1·cm -1. Conditional cons tants were defined, the maximum binding number n=7.The apparent binding ba lance constant K=2.59×10 6. It is found that Scatchard model is appr opriate in the treatment of data obtained here. It is suggested that the electr ostatic force and distant water force are the main binding force between BSA and TB.

关 键 词：牛血清蛋白 百里酚 硫醇 苯并 表观摩尔吸光系数 最大吸收波长 最大吸收峰 平衡透析法 缓冲溶液 相互作用 双波长法 摩尔比法 平衡常数 综合作用 静电引力 复合物 BSA 光谱法 Vis 微环境 结合数 应用 TB 酸性 平均 

分 类 号：O629[理学—有机化学]