本研究旨在研究水稻金属硫蛋白OsMT-1-2a基因原核表达情况及清除活性氧的能力.从水稻中克隆获得的OsMT-1-2a基因亚克隆至pET32a原核表达载体上,在大肠杆菌BL21 (DE3)中成功表达了带有6xHis标签的OsMT-1-2a全长重组蛋白,主要以可溶性蛋白形式存在,分子量大小为32 kD,与预期大小一致.随后,通过镍柱法纯化目的蛋白,利用WST法表明纯化蛋白在体外具有一定的清除超氧化物的能力.“,”This aim of this study was to evaluate the prokaryotic expression and ROS scavengring ability of rice metallothionein protein OsMT-1-2a.OsMT-1-2a gene cloned from rice was transferred to prokaryotic expression vector pET32a to obtain expression vector pET32a-OsMT-1-2a,then the OsMT-1-2a full length recombinant protein with a 6xHis label was successfully expressed in Escherichia coli strain BL21 (DE3).The fused protein mainly existing as soluble protein,was about 32 kD in molecular weight,being in line with the expected size.Using WST method,the fusion OsMT-1-2a protein purified with NI-NTA was found to have an ability in scavengering superoxide anion in vivo.