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Heterologous expression of bovine lactoferricin in Escherichia coli

机译:牛乳铁蛋白在大肠杆菌中的异源表达

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According to the bias of codon utilization of Escherichia coli, a fragment encoding bovine lactoferricin(LfcinB) has been cloned and expressed in the Escherichia coli under the control of the T7 promoter. The target peptide was expressed by IPTG induction, purified by affinity chromatography with 6XHis tagged resin. The recombinant bovine lactoferricin appears to be successfully expressed, as it displays antibacterial activity (antibacterial assay). Moreover, the identity of the recombinant product was estimated by Tricine-SDS-PAGE.
机译:根据大肠杆菌密码子利用的偏向,已克隆了编码牛乳铁蛋白(LfcinB)的片段,并在T7启动子的控制下在大肠杆菌中表达。通过IPTG诱导表达目标肽,通过用6XHis标记的树脂的亲和色谱法纯化。重组牛乳铁蛋白似乎已成功表达,因为它具有抗菌活性(抗菌测定)。此外,通过Tricine-SDS-PAGE估计重组产物的身份。

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