Abstract
The production of heterologous protein, including recombinant antibody derivatives like scFv, in the periplasmic space of E. coli is accomplished by correct signal sequence processing, formation of disulfide bridges and can therefore lead to soluble functional recombinant product. But the yield of functional, soluble recombinant protein from E. coli is often drastically limited by growth inhibition due to a toxic effect of the product and protein aggregation. In accordance with other investigators concerning scFv expression in E. coli we found that in the periplasm only a constant threshold concentration of soluble recombinant protein can be reached. Moreover this threshold concentration is dependent on the individual V-regions and can not be significantly influenced by promoter strength and culture conditions (Rippmann et al., 1998).
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© 2001 Springer-Verlag Berlin Heidelberg
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Moosmayer, D., Rippmann, J.F. (2001). Expression of scFv in L-Form Bacteria. In: Kontermann, R., Dübel, S. (eds) Antibody Engineering. Springer Lab Manuals. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-04605-0_19
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DOI: https://doi.org/10.1007/978-3-662-04605-0_19
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-41354-7
Online ISBN: 978-3-662-04605-0
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