【摘要】 用衰减全反射(ATR)傅立叶变换红外光谱技术研究了重组人铜锌SOD(rhCu,Zn-SOD)在脱水过程中的二级结构变化及保护剂的作用。结果显示,在脱水过程中,蛋白质结构发生了重排,无论是真空干燥还是冷冻干燥,子峰峰位都发生偏移,α-螺旋结构消失,产生无规卷曲结构。糖和硼酸盐能够有效地维持酶的天然构象,其中海藻糖对冻干过程中rhCu,Zn-SOD的α-螺旋结构维持率为93%。更多还原

【Abstract】 In this work, with attenuated total reflection fouriertransform infared spectroscopy (ATR FTIR), structural changes in rhCu,ZnSOD induced by dehydration(freezedrying and vacuumdrying)and the relationship between conformational stability and protectives were investigated. ATR FTIR is proved to be a valuable method in examining structural information of rhCu,ZnSOD in solution or dried state. The protein undergoes significant changes in the secondary structure upon freezedrying and vacuumdrying. Being dehydrated, the band positions shifted, αhelix in solution disappeared and a great amount of random coil appeared. The addition of carbohydrates and borate inhibited the protein secondary rearrangements. The efficiency can be reflected by the retain of αhelix. Trehalose appeares to be the most efficient protective. Its maintenance of αhelix upon freezedrying is 93%.更多还原