化学学报 ›› 2000, Vol. 58 ›› Issue (12): 1649-1653. 上一篇    下一篇

研究论文

丝裂霉素C与牛血清蛋白结合作用的研究

易平贵;商志才;俞庆森;邵爽;林瑞森   

  1. 湘潭工学院化工系;浙江大学化学系.杭州(310027)
  • 发布日期:2000-12-15

Studies on the interaction between mytomycin C and bovine serum albumin

Yi Pinggui;Shang Zhicai;Yu Qingsen;Shao Shuang;Lin Ruisen   

  1. Zhejiang Univ, Dept Chem.Hangzhou(310027)
  • Published:2000-12-15

结合光谱法与微量热法研究了水溶液中丝裂霉素C与牛血清白蛋白分子间的结合反应,测定了反应的结合常数K~A,结合位点数n及热力学函数△~rG~m,△~rH~m和△~rS~m,并确定了分子间作用力性质;依据Forster非辐射能量转移机制,确定了授体-受体间的结合距离和能量转移效率;采用同步荧光技术考察了丝裂霉素C对牛血清白蛋白构象的影响。

关键词: 丝裂霉素C, 血清白蛋白, 量热法, 热力学函数, 构象

The binding characteristics of mytomycin C (MMC) with bovine serum albumin (BSA) have been studied by fluorescence spectroscopy and microcalorimetry method in aqueous solution. The equilibrium constant K~A, the number of binding sites n, and the thermodynamic functions for the reaction have all been measured. The binding distance between MMC and BSA and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer. the effect of MMC on the conformation of BSA has also been analyzed using synchronous fluorescence spectroscopy.

Key words: MUTAGENS, SERUM ALBUMIN, CALORIMETRY, THERMODYNAMIC FUNCTION, CONFORMATION

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