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作 者:袁向华[1]
机构地区:[1]西华师范大学生命科学学院,四川南充637002
出 处:《西华师范大学学报(自然科学版)》2005年第3期298-301,共4页Journal of China West Normal University(Natural Sciences)
基 金:西华师范大学科研启动基金(2004)
摘 要:为了探明重金属Hg2+进入体内,对血清蛋白固有结构和功能的影响,我们用Hg2+对NBS修饰前后血清蛋白HSA和BSA进行处理,然后分析血清蛋白的圆二色谱特性.结果表明,近紫外区未修饰的HSA和BSA均具有典型的α螺旋构象;Hg2+处理或NBS修饰BSA溶液,均引起α-螺旋含量减少和三级结构构象的改变.Hg2+处理HSA,α-螺旋含量略有增加,构象也有变化.而NBS修饰导致α簇结构的严重破坏,蛋白构象无序化程度加深.修饰对BSA、HSA光谱特性的影响不同,可能与这两种蛋白的结构差异有关.In this paper, the effects of Hg^2+ on the CD of serum albumin with or without NBS modification were investigated. The CD spectra measurement showed that the far-UV regions of non-modified HSA and BSA both had typical α-helix. Hg^2+ treatment or NBS modification changed the content of secondary structure and conformation of BSA. Hg^2+ affected little on far-UV CD spectra of HSA, indicating little changes of secondary structure in this protein. However, NBS modification influenced on near-UV structural configuration greatly and Hg^2+ also changed the configuration markedly. The fact that modifications had different effects upon CD spectra of BSA and HSA is probably relative to the structural difference of the two proteins.
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