کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359272 | 1542289 | 2018 | 33 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Highly efficient production of functional recombinant human fibroblast growth factor 22 in E. coli and its protective effects on H2O2-lesioned L02â¯cells
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کلمات کلیدی
PTZGdnHClFGF receptorsFGFRBCAFGFDTTIPTGDMEMDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده DulbeccoMTT - MTTROS - ROSProtective effects - اثرات محافظتیinclusion body - بدن درگیرbicinchoninic acid - بیسینکنینیک اسیدdithiothreitol - دیتیوتریتولlactate dehydrogenase - لاکتات دهیدروژناز LDH - لاکتات دهیدروژناز به صورت مختصر شده LDH methylthiazol tetrazolium - متیل تیتازول تترازولیمpentylenetetrazol - پنتیلن تترازولGuanidine hydrochloride - گوانیدین هیدروکلرایدReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In the 22 member mammalian FGF family, FGF22 belongs to FGF7 subfamily, and its effects are largely confined to the brain and skin. To explore the functions of FGF22 on other tissues and develop a large-scale production of recombinant human FGF22 (rhFGF22) without a fusion tag, a plasmid encoding human FGF22 (pET3a-rhFGF22) was used to express rhFGF22 in E. coli BL21 (DE3) pLysS. A large amount of rhFGF22 inclusion body protein was obtained. A two-step denaturing method successfully solubilized rhFGF22, and it was refolded and then purified in one step via heparin affinity chromatography. A yield of 105â¯mg rhFGF22 with a purity of up to 95% was obtained from 100â¯g wet bacteria. It was found that the rhFGF22 had biological activity, since it effectively attenuated H2O2-induced human hepatic L02â¯cell death. Analysis by qRT-PCR and Western blot demonstrated that rhFGF22 protects L02â¯cells from H2O2-induced oxidative damage via suppression of mitochondrial apoptosis pathways. In conclusion, the strategy described in this paper may provide a novel means to solve the production of insoluble rhFGF22 and shine new light on its translational potential.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 152, December 2018, Pages 114-121
Journal: Protein Expression and Purification - Volume 152, December 2018, Pages 114-121
نویسندگان
Huanhuan Yang, Haishan Tian, Jiliang Cheng, Jie Zheng, Dezhong Wang, Changye Sun, David Fernig, Taotao Chen, Weiyue Gong, Shen Wang, Xiaokun Li, Chao Jiang,