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Staphylokinase as a plasminogen activator component in recombinant fusion proteins

Article Abstract:

Research was conducted to evaluate the use of staphylokinase (SAK) as a plasminogen activator component in recombinant fusion proteins. Both N- and C-terminal fusions to SAK were developed using hirudin as a fusion partner. Recombinant fusion proteins were then secreted from Bacillus subtilis and purified from culture supernatants. Results indicate that C-terminal fusions represent stable configurations for constructing improved thrombolytic agents based on SAK as the plasminogen activator component.

Author: Szarka, S.J., Sihota, E.G., Habibi, H.R., Wong, S.-L.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Plasminogen activators, Fibrinolytic agents, Bacterial proteins

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Multiple microfermentor battery: A versatile tool for use with automated parallel cultures of microorganisms producing recombinant proteins and for optimization of cultivation protocols

Article Abstract:

The design and basic operation of a multiple microfermentor battery comprising of eight miniature bioreactors whose culture parameters could be controlled independently is described. It is found that this microfermentor is well suited for automated parallel cultures and process optimization, such as that needed for structural genomics projects.

Author: Franchon, Emmanuel, Bondet, Vincent, Munier-Lehmann, Helene, Bellalou, Jacques
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
Science & research, Physiological aspects, Microorganisms

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Compatible-solute-supported periplasmic expression of functional recombinant proteins under stress conditions

Article Abstract:

Researchers describe a technique for producing recombinant proteins that can be done at high salt concentrations. It involves using compatible solutes that not only protect the bacterium but also produce a periplasmic microenvironment to generate high levels of correctly folded recombinant proteins.

Author: Barth, S., Huhn, M., Matthey, B., Klimka, A., Galinski, E.A., Engert, A.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Proteins, Protein synthesis

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Subjects list: Research, Recombinant proteins
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