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l-Arginine Suppresses Aggregation of Recombinant Growth Hormones in Refolding Process from E. coli Inclusion Bodies

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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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Abbreviations

SEC:

Size exclusion chromatography

mGH:

Recombinant mink growth hormone

pGH:

Recombinant porcine growth hormone

hGH:

Recombinant human growth hormone

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Authors and Affiliations

  1. Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, 10223, Vilnius-40, Lithuania

    Egle Bajorunaite, Jolanta Sereikaite & Vladas-Algirdas Bumelis

Authors
  1. Egle Bajorunaite
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  2. Jolanta Sereikaite
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  3. Vladas-Algirdas Bumelis
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Correspondence to Jolanta Sereikaite.

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Bajorunaite, E., Sereikaite, J. & Bumelis, VA. l-Arginine Suppresses Aggregation of Recombinant Growth Hormones in Refolding Process from E. coli Inclusion Bodies. Protein J 26, 547–555 (2007). https://doi.org/10.1007/s10930-007-9096-x

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  • DOI: https://doi.org/10.1007/s10930-007-9096-x

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