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学科主题: 生命有机化学
题名: Overexpression in escherichia coli and characterization of the chloroplast fructose-1,6-bisphosphatase from wheat.
其他题名: 小麦叶绿体果糖-1,6-二磷酸酯酶在大肠杆菌中的高表达及其性能测定
作者: Tang GL(唐功利) ; Wang YF(王燕芳) ; Bao JS(鲍建绍) ; Chen HB(陈海宝)
通讯作者: 陈海宝
刊名: Protein Expr. Purif.
发表日期: 2000-01-01
卷: 19, 期:3, 页:411-418
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机化学实验室
英文摘要: An important calvin cycle enzyme, chloroplast fructose-1,6-bisphophatase (FBPase) from wheat, has been cloned and expressed up to 15% of the total cell protein using a pOLc expression vectro in escherichia coli by replacing the codons in the 5'-terminal encoding sequence with optimal and A/T-rich ones. The overexpressed wheat FBP ase is soluble, fully active, and heat stable. It can be purified by chromatography in trun on DEAE-Sepharose and sephacryl S-200, and around 15 mg of purified enzymes (>95%) is obtained from 1 liter of cultured bacteria. Its special activity is 8.8 u/mg, Kcat is 22.9/S, Km is 121 μM, and V max is 128 μmol/min.mg. The recombinant FBPase can be activated by DTT, Na~+, or low concentrations of Li~+, Ca~2+, Zn~2+, GuHCl, and urea, while it can be inhibited by K+ or NH~+^4.
语种: 英语
相关网址: 查看原文
内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/25739
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Tang GL,Wang YF,Bao JS,et al. Overexpression in escherichia coli and characterization of the chloroplast fructose-1,6-bisphosphatase from wheat.[J]. Protein Expr. Purif.,2000,19(3):411-418.
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