Optimization of recombinant ß-NGF purification using immobilized metal affinity chromatography
作者: Zahra HajihassanMehri AbdiElaheh Roshani YasaghiAzra Rabbani-Chadegani
刊名: Minerva Biotecnologica, 2017, Vol.29 (3)
来源数据库: ProQuest Journal
原始语种摘要: BACKGROUND: Several proteins have been purified in a single step from E. coli using fused histidine tails and immobilized metal affinity chromatography (IMAC). Many attempts have been done in order to optimize protein purification by this method. METHODS: As the efficiency of purification is dependent on buffers and conditions used, so in this study different pH, imidazole concentration and incubation time were surveyed to optimize recombinant β-NGF purification. RESULTS: In this work pET39b vector containing DsbA sequence was used in order to produce recombinant β-NGF with his tag tails; β-NGF is produced in the form of DsbA-βNGF fusion by using this vector. Also in order to determine the secondary structure and function of purified β-NGF, CD spectroscopy and treatment of PC12 cell...
全文获取路径: ProQuest  (合作)
影响因子:0.379 (2012)

  • recombinant 重组体
  • purification 提纯
  • NGF Navigation Flare
  • purified 净化的
  • affinity 亲和力
  • proteins 蛋白质
  • functional 功能的
  • metal 金属
  • concentration 浓度
  • fully 充分