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首页> 外文期刊>Protein Expression and Purification >Periplasmic expression and recovery of human interferon gamma in Escherichia coli
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Periplasmic expression and recovery of human interferon gamma in Escherichia coli

机译：人干扰素γ在大肠杆菌中的周质表达和恢复

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摘要

A synthetic human interferon gamma (hIFN-gamma) gene was fused to SP1 and SP3, two See-dependent artificial signal peptides to transport the hIFN-gamma to the periplasm of Escherichia coli BL21-SI. The processing efficiency of both SP1-hIFN-gamma and SP3-hIFN-gamma was dependent on the culture medium as well as the post-induction temperature. Both precursors were processed completely when cells were cultured using minimal medium and a post-induction temperature of 32.5 degrees C, and only the processed hIFN-gamma was detected. The SP3 signal peptide was more efficient than SPI for the secretion of hIFN-gamma. Sixty percent of the total hIFN-gamma was secreted to the periplasm using the SP3 signal peptide and a post-induction temperature of 20 degrees C. Using Tris-sucrose-dithiothreitol (TSD) hypertonic buffer, the periplasmic soluble hINF-gamma was recovered with a purity of 85%. (C) 2008 Elsevier Inc. All rights reserved.
机译：将合成的人干扰素γ（hIFN-γ）基因融合到SP1和SP3，这两个See依赖性人工信号肽可将hIFN-γ转运至大肠杆菌BL21-SI的周质。 SP1-hIFN-γ和SP3-hIFN-γ的加工效率都取决于培养基以及诱导后的温度。当使用最少的培养基和32.5摄氏度的诱导后温度培养细胞时，两种前体均被完全加工，并且仅检测到加工过的hIFN-γ。 SP3信号肽比SPI更有效地分泌hIFN-γ。使用SP3信号肽和诱导后温度20摄氏度，将60％的hIFN-γ分泌到周质中。使用Tris-蔗糖-二硫苏糖醇（TSD）高渗缓冲液，用纯度为85％。 （C）2008 Elsevier Inc.保留所有权利。

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