【摘要】 经丙酮分级沉淀,DEAE-琼脂糖离子交换层析和Sephacry1S-200凝胶过滤,从黄鳝内脏中分离纯化获得铁超氧化物歧化酶(Fe-SOD),并对其部分性质进行分析鉴定。获得该酶的比活力为1500U mg,提纯倍数为368 5,回收率为24 7%。该酶最大紫外吸收波长为280nm。聚丙烯酰胺凝胶电泳和等电点聚焦电泳结果表明纯化酶蛋白呈一条带,测得该酶分子量约为87kD,亚基分子量约为14 5kD;等电点为pH7 1。更多还原

【Abstract】 Superoxide dismustase was isolated and purified from ricefield eel Monopterus albus by grading precipitation with acetone, DEAE-Sepharose chromatography and Sephacry1 S-200 gel filtration. The results showed that the specific activity of the enzyme was 1500 units per mg protein with purification factor of 368.5 and the yield of 24.7. It had the absorption maximum in the ultraviolet at 280 nm and one protein band by SDS-PAGE and isoelectric focusing (IEF). The enzyme had a molecular weight of 87 000 daltons with isoelectric point of pH 7.1 by gel filtration on Sephacry1 S-200 and subunits of 14 500 daltons by SDS-PAGE.更多还原