Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Heike Mikschofsky"'
Publikováno v:
PLoS ONE, Vol 8, Iss 5 (2013)
Externí odkaz:
https://doaj.org/article/44418c7c889c404b904a94c9fbacc608
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e54933 (2013)
In this study, we compared basic expression approaches for the efficient expression of bioactive recombinant human interleukin-6 (IL6), as an example for a difficult-to-express protein. We tested these approaches in a laboratory scale in order to pio
Externí odkaz:
https://doaj.org/article/76c15b40962a4a229fbd2a58c42c6acb
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e48938 (2012)
Tobacco plants can be used to express recombinant proteins that cannot be produced in a soluble and active form using traditional platforms such as Escherichia coli. We therefore expressed the human glycoprotein interleukin 6 (IL6) in two commercial
Externí odkaz:
https://doaj.org/article/f58ec409210c4e2480a78d44bdc7ac81
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e53023 (2012)
We evaluated transgenic tobacco plants as an alternative to Escherichia coli for the production of recombinant human complement factor 5a (C5a). C5a has not been expressed in plants before and is highly unstable in vivo in its native form, so it was
Externí odkaz:
https://doaj.org/article/3bb2498924f14e3c92c18928e4387d6d
Autor:
Kerstin Schmidt, Christine Höflich, Mandy Bruch, Kristin Entzian, Patricia Horn, Andre Kacholdt, Udo Kragl, Peter Leinweber, Heike Mikschofsky, Wenke Mönkemeyer, Elmar Mohr, Katja Neubauer, André Schlichting, Jörg Schmidtke, Alain Steinmann, Carla Struzyna-Schulze, Ralf Wilhelm, Annette Zeyner, Angelika Ziegler, Inge Broer
Publikováno v:
Journal für Kulturpflanzen, Vol 63, Iss 7 (2011)
Genetically modified (GM) plants have to be analyzed for their potential impacts on the environment and on human or animal health before authorisation by the EU. The approval process currently refers to a conglomeration of diverse analytical metho
Externí odkaz:
https://doaj.org/article/47f69887ba9c437f938ed70b74e56ea1
Autor:
Henrik Nausch, Inge Broer, Jana Huckauf, Alain Steinmann, Udo Meyer, Roswitha Koslowski, Heike Mikschofsky
Publikováno v:
African Journal of Biotechnology; Vol 12, No 3 (2013)
A major limitation of plant bioreactors is the lack of suitable and cost-effective purification methods for the extraction of pharmaceutical-grade proteins. In contrast to that, there are numerous established purification systems for heterologous pro
Autor:
Inge Broer, Heike Mikschofsky
Publikováno v:
Transgenic Research. 21:715-724
Based on its high protein content and excellent storage capacity, pea (Pisum sativum), as well as other plants, is considered to be a suitable production platform for protein-based pharmaceuticals. Its capacity to produce high proportions of active r
Autor:
Inge Broer, Peter Leinweber, Heike Mikschofsky, Jörg Schmidtke, Elena Heilmann, Kerstin Schmidt, Udo Meyer
Publikováno v:
Plant Molecular Biology. 76:131-144
The production of plant-derived pharmaceuticals essentially requires stable concentrations of plant constituents, especially recombinant proteins; nonetheless, soil and seasonal variations might drastically interfere with this stability. In addition,
Autor:
Kerstin Schmidt, Günther M. Keil, Jörg Schmidtke, Inge Broer, Heike Mikschofsky, Anja Hartmann, Patricia König, Wolfgang B. Souffrant, Manfred Schwerin, Pawel Janczyk, Martin Hammer, Holger Junghans, Horst Schirrmeier
Publikováno v:
Food and Nutrition Sciences. :74-86
Recombinant plant-derived pharmaceuticals have been investigated for the last two decades and some products will soon be brought to market. Since veterinary pharmaceuticals seem to be the front-runners of plant-derived vaccines, we selected one model
Autor:
Patricia L. Polowick, Inge Broer, Horst Schirrmeier, Heike Mikschofsky, Wilf Keller, Bodo Lange, Günther M. Keil
Publikováno v:
Plant Biotechnology Journal. 7:537-549
Vaccines against rabbit haemorrhagic disease virus (RHDV) are commercially produced in experimentally infected rabbits. A genetically engineered and manufactured version of the major structural protein of RHDV (VP60) is considered to be an alternativ