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利用紫外差吸收光谱和荧光发射光谱等监测手段研究天然铜锌ＳＯＤ（ｈｏｌｏ－ＳＯＤ）和脱铜锌ＳＯＤ（ａｐｏ－ＳＯＤ）在不同浓度胍溶液中的去折叠及活力变化．结果表明ｈｏｌｏ－ＳＯＤ和ａｐｏ－ＳＯＤ分别在４．０和２．０ｍｏｌ／Ｌ胍溶液中去折叠，而分别在２．０和０．５ｍｏｌ／Ｌ胍溶液中其构象尚未发生明显改变时活性几乎完全丧失．提示金属离子对维持酶的整体及活性部位构象具有重要作用，脱去金属离子的酶分子的构象特别是活性部位的构象更易受到变性剂的破坏．
The de-folding and vitality changes of holo-SOD and apo-SOD in different concentrations of guanidine solution were investigated by means of ultraviolet absorption spectroscopy and fluorescence emission spectroscopy. The results showed that the holo-SOD and apo-SOD were unfolded in 4.0 and 2.0 mol / L guanidine solution, respectively, while their conformations had not changed significantly in 2.0 and 0.5 mol / L guanidine solution respectively Completely lost. It is suggested that the metal ions play an important role in maintaining the overall conformation of the enzyme and the conformation of the active site. The conformation of the enzyme molecule that has taken off the metal ion, especially the conformation of the active site, is more likely to be damaged by the denaturant.