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首页> 外文期刊>Preparative biochemistry & biotechnology: An international journal for rapid communication >Fusion expression of human beta-defensin-2 from multiple joined genes in Escherichia coli
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Fusion expression of human beta-defensin-2 from multiple joined genes in Escherichia coli

机译：人β-防御素2在大肠杆菌中多个连接基因的融合表达

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摘要

Human beta-defensin-2 (hBD-2) is a cysteine-rich cationic low molecular weight antimicrobial peptide, which exhibits a broad range of antimicrobial activity without observed acquired resistance. In this work, multiple copies of the hBD-2 gene were linked in tandem and the expression of the multiple joined genes in two fusion expression system, pET28a(+) and pGEX-4T-2, was examined. Using plasmid pET28a(+) with one, two, and four copies of the hBD-2 gene, the expressed level was relatively low, whereas much higher with plasmid pGEX-4T-2, and the fusion products, most of which in insoluble form, account for approximately 26% of the total insoluble cellular proteins.
机译：人β-防御素2（hBD-2）是富含半胱氨酸的阳离子低分子量抗微生物肽，在没有观察到的获得性耐药性的情况下表现出广泛的抗微生物活性。在这项工作中，hBD-2基因的多个副本串联在一起，并检查了两个融合表达系统pET28a（+）和pGEX-4T-2中多个连接基因的表达。使用带有1、2和4个hBD-2基因拷贝的质粒pET28a（+），表达水平相对较低，而质粒pGEX-4T-2及其融合产物的表达水平要高得多，其中大多数为不溶形式，约占总不溶细胞蛋白的26％。

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