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不同来源的超氧化物歧化酶（SOD）的克隆已有报道，用RT－PCR方法我们成功地从大鼠晶体上皮细胞中克隆出了CU－ZnSODcDNA并利用pMal载体在大肠杆菌中高效表达出MBP－SOD融合蛋白可占菌体总蛋白40％左右，采用的蛋白纯化系统的亲和层析柱就是利用的MBP融合蛋白可被快速纯化而设计的，实验证明此方法可快捷、高效地表达有生物学活性的MBP—SOD融合蛋白。
Cloning of different sources of superoxide dismutase (SOD) has been reported. Using RT-PCR, we successfully cloned CU-ZnSOD cDNA from rat lens epithelial cells and efficiently expressed MBP in E.coli using pMal vector -SOD fusion protein can account for about 40% of the total bacterial protein. The affinity chromatography column used in the protein purification system is that the utilized MBP fusion protein can be rapidly purified and designed, and the experiment proves that the method can be expressed quickly and efficiently Biologically active MBP-SOD fusion protein.