Title
l-Argininamide improves the refolding more effectively than l-arginine
Author
Hiroyuki Hamada, Kentaro Shiraki
Year
2007
Journal
Journal of Biotechnology
Abstract
l-Arginine (Arg) is a widely used additive for suppressing protein aggregation during refolding. Systematic screening of Arg analogs provides superior additives that enhance the refolding yield more effectively than Arg. The refolding yield of hen egg lysozyme in the presence of 500 mM l-argininamide (ArgAd) increases 1.7-fold higher than Arg. Thermal unfolding experiments indicate that ArgAd has a greater denaturing effect than Arg. The refolding yield positively relates to the net charge of Arg analogs. Moreover ArgAd was also effective for the refolding of bovine carbonic anhydrase. High potency to increase the refolding yield of ArgAd compared to Arg results from high positive net charge and the denaturing property.
Instrument
J-720
Keywords
Circular dichroism, Tertiary structure, Protein denaturation, Thermodynamics, Thermal stability, Biochemistry