金属螯合亲和层析分离纯化重组人锰超氧化物歧化酶  

Resolution and Purification of Recombinant Human Manganese Super-oxide Dismutase by Immobilised Metal Affinity Chromatography

作　　者：廖晓全[1] 张艳红[1] 袁勤生[1] 

机构地区：[1]华东理工大学生物工程学院生物反应器工程国家重点实验室,上海200237

出　　处：《药物生物技术》2002年第3期146-149,共4页Pharmaceutical Biotechnology

摘　　要：以金属铜螯合的亲和层析方法分离纯化重组人锰超氧化物歧化酶,采用3种不同的洗脱方法都可以对重组酶进行分离纯化.但是通过鉴别比较,采用方法1即逐步降低洗脱液的pH和固定洗脱液的NH+4的浓度可以获得较好的结果,SDS-聚丙烯酰胺凝胶电泳得到一条分子质量约为22000u的蛋白条带,证明所得到的为纯度较高的重组人锰超氧化物歧化酶（rhMn-SOD）。Purified the recornbinant human manganese superoxide dismutase by metals-chelating affinity chro-matography(MCAC) . All three kinds of elution methods can purified the recornbinant enzyme. But by comparing the three kinds of methods, used the method one can obtain the best results. That is, decreased the pH of the elution buffer and the concentration of NH4+ is 0. 5mol/L. SDS-PAGE show that the recornbinant human manganese superoxide dismutase was purified homogeneously and the molecular weight of the subunits of the purified enzyme is 22000.

关 键 词：重组人锰超氧化物歧化酶 金属螯合亲和层析 洗脱 纯化 

分 类 号：Q55[生物学—生物化学]