h—SOD在脲、胍变性剂中的光谱学特征

研究了人血超氧化物歧化酶（h-SOD)在脲、胍及不同温度下变性的分子构象与活力之间的关系。酶的吸收光谱与酶活力的变化表明：当用不同的变性剂处理后，酶蛋白的空间结构发生了改变，紫外吸收表现出明显的增色效应；酶的荧光强度随脲浓度的增加有所增加随胍浓度的增加明显下降，在4mol/L胍变性条件下，h-SOD的发射峰自337nm红移到353nm，且酶活力明显下降。据此结果推测：酶活力的下降与构象的改变是同步发生的。

The SpectralCharacteristic of h-SOD in Urea and Guanidine Solution

The denaturation of human superoxide dismutase (h-SOD )in the presence urea and guanidine was measured by fluorescence and ultraviolet spectrum.The fluorescence intensity of enzyme gradually increased with increasi ng urea concentration,and gradually decreased with increasing guanidine concentr ation.The fluorescence emission peak (at 337nm) of h-SOD in 4mol/L guanidine so lution was red-shifted to 353 nm,and the enzyme activity was obvious decreased. It is suggested that the change of enzyme conformation and its activity decrease in different denaturants was occur in the same time.