嗜酸氧化亚铁硫杆菌亚硫酸还原酶的α亚基黄素蛋白(cysJ)的表达、纯化及活性测定  

Expression,Purification and Activity Determination of Flavoprotein(cysJ)-α Subunit of the SiR Protein from Acidithiobacillus Ferrooxidans

作　　者：王敏[1] 曾嘉[1] 黄霞[1] 柳建设[1] 邱冠周[1] 

机构地区：[1]中南大学资源加工与生物工程学院,长沙410083

出　　处：《现代生物医学进展》2008年第3期453-455,470,共4页Progress in Modern Biomedicine

基　　金：国家"973"基金(2004CB619204);国家自然科学创新群体基金(50621063);全国博士学位论文作者专项资金(200549)

摘　　要：亚硫酸还原酶是嗜酸氧化亚铁硫杆菌硫氧化还原系统电子传递链的重要组分之一。本文以嗜酸氧化亚铁硫杆菌ATCC23270基因组为模板,通过基因重组技术在大肠杆菌中表达,用一步亲和层析法纯化出浓度和纯度都较高的亚硫酸还原酶的a亚基黄素蛋白(cysJ)。通过SDS-聚丙烯酰胺凝胶电泳、紫外可见分光光度法等方法确定其性质并成功测定了活性,为进一步研究亚硫酸还原酶的功能及其应用提供了条件。Sulfite Reductase is thought to be a principal component in the sulfur oxidation electron transport chain of Acidithiobacillus ferrooxidans. The gene of flavoprotein （cysJ）-α subunit of the SiR protein from A. ferrooxidans ATCC23270 was cloned, overexpressed and purified by one-step affinity chromatography. The SDS-PAGE and UV-VIS spectrophotometer was used to determine the character and activity of this protein. The result was expected to be helpful for further study in the function and application of the SiR protein.

关 键 词：嗜酸氧化亚铁硫杆菌 亚硫酸还原酶 黄素蛋白 cysJ SiR—FP 

分 类 号：Q512[生物学—生物化学]