کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8359959 | 1542326 | 2015 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression and purification of active recombinant human bone morphogenetic 7-2 dimer fusion protein
ترجمه فارسی عنوان
بیان و تصفیه پروتئین فیوژن 7-2 دی مورفون مورفوژنتیک استخوانی نوترکیب انسان
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
چکیده انگلیسی
Bone morphogenetic proteins (BMPs) have been applied in bone regeneration therapy due to their significant osteogenic activity, however, the complicated processing and high cost in producing recombinant BMP have limited their use in the clinic. In this study, we have developed a simple method to prepare recombinant human BMP7-BMP2 fusion protein with a flexible peptide linker (rhBMP7-2). The rhBMP7-2 protein is expressed efficiently in Escherichia coli, and the denatured protein purified by anion exchange chromatography then refolded by dialysis. The yield was about 6.8Â mg per gram of wet cell weight. The bioactivity of re-folded rhBMP7-2 was measured by alkaline phosphatase assay and alizarin red staining using both C2C12 and MC3T3-E1 cells, and also using the rat subcutaneous ectopic bone formation model. High level osteogenic activity was found in all the assays tested demonstrating the production of corrected folded and active rhBMP7-2 protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 61-68
Journal: Protein Expression and Purification - Volume 115, November 2015, Pages 61-68
نویسندگان
Jianli Dang, Lei Jing, Weiwei Shi, Ping Qin, Yuyin Li, Aipo Diao,