枯草杆菌蛋白酶与茜素氨羧络合剂作用研究  

Study on the Reaction of Proteinase from Bacillus Subtilis with Alizarin Complex

作　　者：王兴明[1] 董发勤[1] 丁立生[2] 杨定明[1] 石荣铭[1] 

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,四川成都610041

出　　处：《光谱学与光谱分析》2005年第9期1471-1474,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金(40072020);四川省教育厅自然科学基金重点(2000A56)资助项目

摘　　要：应用UV光谱法研究在pH4.20的酸性溶液中,枯草杆菌蛋白酶(BSP)与茜素氨羧络合剂(ALC)的相互作用。测得生成的缔合物的最大吸收峰为510nm,与试剂相比红移85nm。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=6.68×103L·mol-1·cm-1,表观结合常数K=7.25×106L·mol-1,平均结合数n=10,与BSP的活性部位基本吻合。研究发现,该反应基本符合Scatchard模型,认为是BSP与ALC之间以电荷力为主、疏水力为辅综合作用的结果。The interaction of bacillus subtilis proteinase（BSP） and Alizarin Complex （ALC） was investigated by spectrophotometric method in acidic solution（pH 4.20）. When BSP was added into ALC, a red color was observed, which indicated the formation of BSPALC associated compound. The maximum absorption of the red color coordination eompound was obtained at 510 nm. It was found that the red shift of maximum absorption of the eomplex was 85 um. Aceording to balance pereolation method, molar ratio method and double wavelengh method, the apparent molar absorptivity εB = 6.68 × 10^3 L·mo1^-1 ·cm^-1. Conditional eonstants were defined, the maximum binding number n = 10, and the apparent binding eonstant K = 7.25 × 10^6 L·mol^-1. It was found that Scatchard model is appropriate in the treatment of data obtained here.

关 键 词：枯草杆菌蛋白酶 茜素氨羧络合剂 作用机理 UV光谱法 透析法 

分 类 号：O614.1[理学—无机化学]