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.
出处
《药物生物技术》
CAS
CSCD
2002年第3期146-149,共4页
Pharmaceutical Biotechnology
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
Recombinant human manganese superoxide dismutase, Immobilised metal-affinity chromato-graphy, Elution, Purification
