کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2022205 | 1069286 | 2006 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Soluble expression of a strong thrombolytic pro-urokinase mutant in Escherichia coli
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
A recombinant pro-urokinase mutant GZ5-sPA was successfully constructed by fusion of a high fibrin-affinity fragment GZ5 to the N-terminus of the serine protease domain of pro-urokinase (sPA). The fragment GZ5 contains a tetrapeptide GPRP and a tripeptide RGD, and was synthesized in bacterial preferred expressing codons. The mutant was then fused to the C-terminus of maltose binding protein (MBP) carried by pMAL-C2x vector, and expressed in Escherichia coli strain Origami (DE3). The produced fusion protein was highly soluble in the cytoplasm of the bacteria. After being cleaved with PreScission Protease to remove MBP tag, GZ5-sPA showed a molecular weight of 31Â kDa on SDS-PAGE. GZ5-sPA maintained the same epitope as wild-type pro-urokinase and possessed a thrombolytic activity three times higher than standard urokinase did after being activated as two-chain form. The results could be a clue to other complicated heterogenous proteins similar to pro-urokinase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 48, Issue 1, July 2006, Pages 69-73
Journal: Protein Expression and Purification - Volume 48, Issue 1, July 2006, Pages 69-73
نویسندگان
Jian Lin, Xiaoyi Yang, Riqiang Deng, Boguang Yu, Huangjie Lai, Weili Sun, Wenyan Wu,