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.
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)
