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蛋白质与肝素之间相互作用的光谱法研究
引用本文:胡勇,扶雄,陈旭东,杨连生. 蛋白质与肝素之间相互作用的光谱法研究[J]. 广东药学院学报, 2011, 27(1): 18-22. DOI: 10.3969/j.issn.1006-8783.2011.01.005
作者姓名:胡勇  扶雄  陈旭东  杨连生
作者单位:1. 广东药学院,食品科学学院,广东,中山,528458
2. 华南理工大学,轻化工研究所,广东,广州,510640
3. 中山大学,化学与化学工程学院,广东,广州,510275
摘    要:
目的 研究牛血清蛋白(BSA)与肝素(HP)在溶液中的相互作用机理.方法 通过共振光散射光谱(RLS)、紫外吸收光谱及荧光光谱来考察BSA与HP相互作用前后的光谱变化,考察体系的分子结合机理.结果 随着HP的持续加入,体系RLS强度迅速增加;BSA在298 nm左右的吸收峰不断升高和蓝移;BSA的荧光强度出现了显著的下...

关 键 词:牛血清蛋白  肝素  相互作用  光谱学研究

Study of binding interaction between bovine serum albumin and heparin by spectroscopy
HU Yong,FU Xiong,CHEN Xu-dong,YANG Lian-sheng. Study of binding interaction between bovine serum albumin and heparin by spectroscopy[J]. Academic Journal of Guangdong College of Pharmacy, 2011, 27(1): 18-22. DOI: 10.3969/j.issn.1006-8783.2011.01.005
Authors:HU Yong  FU Xiong  CHEN Xu-dong  YANG Lian-sheng
Affiliation:1.School of Food Science,Guangdong Pharmaceutical College,Zhongshan,Guangdong 528458,China;2.College of Light Industry and Food Science,South China University of Technology,Guangzhou,Guangdong 510640,China;3.School of Chemistry and Chemical Engineering,Sun Yat-Sen University,Guangzhou Guangdong 510275,China)
Abstract:
Objective To investigate the interaction mechanism of bovine serum albumin (BSA) and heparin (HP) in solution. Methods The spectral changes of resonance light scattering (RLS), UV absorption spectra and fluorescence spectroscopy were analyzed to examine the molecular binding mechanism. Results The RLS intensity increased rapidly as HP was added, and the absorption peak of BSA located at about 298 nm appeared rising and blue shifting. Meanwhile, the fluorescence intensity of BSA declined significantly first and then ascented later. Conclusion HP molecules can form interpolymeric complexes with BSA by electronic and hydrophobic force, which accounts for the increase of the RLS intensity and the change of proteins' structures. Furthermore, the interaction between BSA and HP has a close relationship with the level of HP concentration.
Keywords:bovine serum albumin  heparin  interaction  spectroscopy
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