Ternary System of Solution Additives with Arginine and Salt for Refolding of Beta-Galactosidase |
| |
Authors: | Akiko Fujimoto Atsushi Hirano Kentaro Shiraki |
| |
Institution: | (1) Institute of Applied Physics, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan; |
| |
Abstract: | l-Arginine hydrochloride (Arg HCl) has been used for protein refolding as a universal aggregation suppressor for monomeric
proteins. This paper presents an investigation of the refolding of tetrameric beta-galactosidase (β-gal) using Arg HCl and
other salts. In a binary system using only Arg HCl, the refolding yield of β-gal increased with increasing concentration up
to 0.2 M. However, the refolding yield sharply decreased above this concentration, reaching the level below the control yield
of 5% at 0.5 M and near zero above 0.75 M, an observation unexpected from monomeric proteins. In a ternary system using both
0.2 M Arg HCl and another salt, the refolding yield increased up to 1.5-fold higher than that in the binary system. These
data indicate that aggregation suppressive effects of protein increase with Arg HCl concentration, but also are deleterious
to self-association of the protein. This dual nature of Arg HCl effects may have to be taken into account in its application
for refolding of oligomeric proteins. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|