The recombinant ADI was one-step purified by using nickel chelated agarose gel affinity chromography. SDS-PAGE anaylysis showed it had a mass weight of approximate 49 kDa as was expected, and the activity of purified enzyme is 4.76 U/mg.
利用镍琼脂糖凝胶亲和层析实现了重组ADI的一步纯化,SDS-PAGE分析显示纯化蛋白分子量大小约为49 kDa,与推测大小相符,纯化蛋白比酶活4.76 U/mg。
参考来源 - 重组精氨酸脱亚胺酶的异源表达、纯化及性质研究·2,447,543篇论文数据，部分数据来源于NoteExpress
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