title: L-arginine suppresses aggregation of recombinant growth hormones in refolding process from E. coli inclusion bodies.
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.
authors.affiliation: Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, 10223, Vilnius-40, Lithuania.
authors.forename: Egle
authors.initials: E
authors.lastname: Bajorunaite
authors.forename: Jolanta
authors.initials: J
authors.lastname: Sereikaite
authors.forename: Vladas-Algirdas
authors.initials: VA
authors.lastname: Bumelis
mesh_terms: D000818:Animals; D001120:Arginine / Q000494:pharmacology*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000235:genetics*; D013006:Growth Hormone / Q000378:metabolism*; D002479:Inclusion Bodies / Q000378:metabolism*; D008907:Mink; D011489:Protein Denaturation; D017510:Protein Folding; D012995:Solubility; D013552:Swine