摘要
为获得大量的α心钠素，构建了含α心钠素多拷贝基因的重组表达载体ｐＭａｌ－ｎＡＮＰ．经ＩＰＴＧ诱导后，在Ｅ．ｃｏｌｉＪＭ１０９中稳定表达融合蛋白．优化诱导条件后，重组蛋白主要以可溶形式存在．
α Human atrial natriuretic peptide (ANP) with a strong dilated,hypotensive function,can be used in treatment of many disease.In order to get a large amount of ANP,through the sticky end complementarity of fragments digested by Nsi Ⅰ and Pst Ⅰ,a series of expression vectors containing multi copied ANP gene were constructed in pMal c2 system(pMal nANP).Induced with IPTG,the fusion proteins were expressed constantly in E.coli JM109.After optimized the induction condition,the recombinant protein was almost completely (91%) expressed in a soluble form in cytoplasma.Elution of maltose of a column of amylose affinity resin saturated with proteins in crude cell extract gave a nearly pure fusion protein.The purified fusion protein successfully caused dilation of previous contracted rat aorta slice,which means it has a better biological activity.
出处
《中国生物化学与分子生物学报》
CAS
CSCD
1999年第3期383-386,共4页
Chinese Journal of Biochemistry and Molecular Biology
基金
国家"八六三"基金
