The Protein Journal

, Volume 26, Issue 8, pp 547–555

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

  • Egle Bajorunaite
  • Jolanta Sereikaite
  • Vladas-Algirdas Bumelis
Article

DOI: 10.1007/s10930-007-9096-x

Cite this article as:
Bajorunaite, E., Sereikaite, J. & Bumelis, VA. Protein J (2007) 26: 547. doi:10.1007/s10930-007-9096-x

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.

Keywords

l-Arginine Recombinant growth hormones Refolding Aggregation 

Abbreviations

SEC

Size exclusion chromatography

mGH

Recombinant mink growth hormone

pGH

Recombinant porcine growth hormone

hGH

Recombinant human growth hormone

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  • Egle Bajorunaite
    • 1
  • Jolanta Sereikaite
    • 1
  • Vladas-Algirdas Bumelis
    • 1
  1. 1.Department of Chemistry and Bioengineering, Faculty of Fundamental SciencesVilnius Gediminas Technical UniversityVilnius-40Lithuania