摘要
将诱导表达的His-hepcidin融合蛋白包涵体通过固定化金属离子配体亲和层析(IMAC)柱分离纯化后,在cys-teine/cystine氧化还原体系中氧化形成二硫键,稀释复性后用肠激酶将融合蛋白的his-tag切除。酶切后所得的Hepcidin经抑菌圈试验检验,对枯草芽孢杆菌等革兰氏阳性菌和部分革兰氏阴性菌具有抗菌活性。
After isolation and purification with the IMAC column, the His-hepcidin fusion protein was oxidized and renaturated in cysteine/cystine system to form disulfide bond. The his-tag was excised by enterokinase and the purity Hepcidin protein was up to 90%. Through agar diffusion assay, the recombinant hepciitin displayed obvious antibacterial activity against Gram bacteria such as B. subtilis and some negative bacteria.
出处
《生物技术通报》
CAS
CSCD
北大核心
2010年第5期192-195,共4页
Biotechnology Bulletin
基金
河南省高新领域重点攻关计划项目(082102220002)
