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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
L-arginine suppresses aggregation of recombinant growth hormones in refolding process from E. coli inclusion bodies
Egle Bajorunaite1, Jolanta Sereikaite, Vladas-Algirdas Bumelis
1Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, 10223, Vilnius-40, Lithuania.
Abstract:
L-Arginine was used to suppress the aggregation of recombinant mink and porcine growth hormones in the refolding process from E. coli inclusion bodies by solubilization-dilution protocol at high protein concentration and pH 8.0. The influence of L-arginine concentration on the renaturation yield of both proteins was investigated. L-Arginine effectively suppressed the precipitation of growth hormones during dilution, but did not inhibit soluble oligomers formation. The results of mink and porcine growth hormones purification from 4 g of biomass are presented.
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