Purification, refolding, and characterization of recombinant LHRH-T multimer.

Abstract

To make the native LHRH immunogenic, a multimer of LHRH interspersed with T non-B peptides (r-LHRH-d2) was expressed as recombinant protein in Escherichia coli. The expression level of the recombinant protein was around 15% of the total cellular protein and it aggregated as inclusion bodies. Inclusion bodies from the bacterial cells were isolated and… (More)

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Cite this paper

@article{Raina2004PurificationRA, title={Purification, refolding, and characterization of recombinant LHRH-T multimer.}, author={Komal Raina and Amulya Kumar Panda and Mushir M Ali and Gursaran Pran Talwar}, journal={Protein expression and purification}, year={2004}, volume={37 1}, pages={8-17} }