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在大肠杆菌RecA+菌株中增强pL控制的重组蛋白生产及质粒稳定性。

Enhanced production of pL-controlled recombinant proteins and plasmid stability in Escherichia coli RecA+ strains.

作者信息

Benito A, Vidal M, Villaverde A

机构信息

Institut de Biologia Fonamental and Departament de Genètica i Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, Spain.

出版信息

J Biotechnol. 1993 Jun;29(3):299-306. doi: 10.1016/0168-1656(93)90061-q.

Abstract

Overexpression of pL-controlled foot-and-mouth disease virus recombinant proteins was studied in Escherichia coli RecA+ strains and in a recA mutant. Higher protein yield and extractable plasmid DNA amounts were found in wild type cells, in absence of detectable RecA proteolytic activity. Minor but still significant differences in pBR322 DNA amounts were also detected between RecA+ and its recA13 and lexA1 derivatives. These data should be seriously considered to select expression systems and to design production processes for recombinant proteins, specially if they are expected to be toxic for Escherichia coli cells.

摘要

在大肠杆菌RecA+菌株和recA突变体中研究了pL控制的口蹄疫病毒重组蛋白的过表达情况。在野生型细胞中,在没有可检测到的RecA蛋白水解活性的情况下,发现了更高的蛋白质产量和可提取的质粒DNA量。在RecA+及其recA13和lexA1衍生物之间,还检测到pBR322 DNA量存在微小但仍显著的差异。在选择表达系统和设计重组蛋白的生产工艺时,应认真考虑这些数据,特别是当预期重组蛋白对大肠杆菌细胞有毒性时。

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