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One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and Triton X-100

Article Abstract:

Research was conducted to examine the construction and expression of a secreted form of single-chain fusion protein sFV/tumor necrosis factor (TNF)-alpha in Escherichia coli using recombinant DNA techniques. The experiment illustrates dramatic enhancement of the excretion of the heterologous fusion protein from E. coli into culture media by the synergistic effect of glycine and Triton X-100. Results support a large-scale method for more efficient production of the heterologus fusion protein sFV/TNF-alpha.

Author: Yang, Junbao, Moyana, Terence, MacKenzie, Samuel, Xia, Qun, Xiang, Jim
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Tumor necrosis factor, Glycine

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Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli

Article Abstract:

An efficient protein secretion system was established by genetically improving the alpha-hemolysin (HlyA) secretion system and by mutagenizing hlyB and hlyD, two HlyB mutants were successfully obtained that have higher levels of secretion activity. One mutant was found to have seven point mutations in both HlyB and HlyD , and an L448F substitution in HlyB was responsible for the improved secretion activity.

Author: Sugamata, Yosuhiro, Shiba, Toshikazu
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Science & research, Mutagenesis

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Secretion of recombinant proteins via the chaperone/usher pathway in Escherichia coli

Article Abstract:

Researchers describe the production of recombinant proteins in E. coli using the Caf1M chaperone/Caf1A usher pathway of Yersinia pestis. This pathway can transport subunits with large heterogeneous N-terminal fusions to the periplasm and cell surface.

Author: Zavialov, Anton V., Batchikova, Natalia V., Korpela, Timo, Petrovskaya, Lada E., Korobko, Vyacheslav G., Kersley, Joanne, MacIntyre, Sheila, Zav'Yalov, Vladimir P.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001

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Subjects list: Research, Escherichia coli, Recombinant proteins
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