Int. J. Mol. Sci. 2011, 12(5), 2808-2821; doi:10.3390/ijms12052808
Article

Membrane-Based Inverse Transition Cycling: An Improved Means for Purifying Plant-Derived Recombinant Protein-Elastin-Like Polypeptide Fusions

Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstrasse 3, Gatersleben 06466, Germany
* Author to whom correspondence should be addressed.
Received: 18 March 2011; in revised form: 11 April 2011 / Accepted: 11 April 2011 / Published: 29 April 2011
(This article belongs to the Special Issue Plant-Derived Pharmaceuticals by Molecular Farming)
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Abstract: Elastin-like peptide (ELP) was fused to two different avian flu H5N1 antigens and expressed in transgenic tobacco plants. The presence of the ELP tag enhanced the accumulation of the heterologous proteins in the tobacco leaves. An effective membrane-based Inverse Transition Cycling was developed to recover the ELPylated antigens and antibodies from plant material. The functionality of both the ELPylated neuraminidase and an ELPylated nanobody was demonstrated.
Keywords: transgenic plants; avian influenza; H5N1; nanobody; ELPylation; Inverse Transition Cycling

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MDPI and ACS Style

Phan, H.T.; Conrad, U. Membrane-Based Inverse Transition Cycling: An Improved Means for Purifying Plant-Derived Recombinant Protein-Elastin-Like Polypeptide Fusions. Int. J. Mol. Sci. 2011, 12, 2808-2821.

AMA Style

Phan HT, Conrad U. Membrane-Based Inverse Transition Cycling: An Improved Means for Purifying Plant-Derived Recombinant Protein-Elastin-Like Polypeptide Fusions. International Journal of Molecular Sciences. 2011; 12(5):2808-2821.

Chicago/Turabian Style

Phan, Hoang Trong; Conrad, Udo. 2011. "Membrane-Based Inverse Transition Cycling: An Improved Means for Purifying Plant-Derived Recombinant Protein-Elastin-Like Polypeptide Fusions." Int. J. Mol. Sci. 12, no. 5: 2808-2821.

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