Bajorunaite Egle, Sereikaite Jolanta, Bumelis Vladas-Algirdas
Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, 10223, Vilnius-40, Lithuania.
Protein J. 2007 Dec;26(8):547-55. doi: 10.1007/s10930-007-9096-x.
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.
