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Recombinant Production, Isotope Labeling and Purification of ENOD40B: A Plant Peptide Hormone

[ Vol. 19 , Issue. 8 ]


Young Kee Chae, Marco Tonneli and John L. Markley   Pages 808 - 811 ( 4 )


The plant peptide hormone ENOD40B was produced in a protein production strain of Escherichia coli harboring an induction controller plasmid (Rosetta(DE3)pLysS) as a His6-tagged ubiquitin fusion protein. The fusion protein product was denatured and refolded as part of the isolation procedure and purified by immobilized metal ion chromatography. The peptide hormone was released from its fusion partner by adding yeast ubiquitin hydrolase (YUH) and subsequently purified by reversed phase chromatography. The purity of the resulting peptide fragment was assayed by MALDITOF mass spectrometry and NMR spectroscopy. The final yields of the target peptide were 7.0 mg per liter of LB medium and 3.4 mg per liter of minimal medium.


Peptide hormone, nodule development, ubiquitin fusion, MS, NMR, symbiosis, nitrogenfixing bacteria (rhizobia), Oligosaccharides, Nod factors, ENOD40


Department of Chemistry and Institute for Chemical Biology, Sejong University, Seoul 143-747, Korea.

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