title: Glutathione ethylester, a novel protein refolding reagent, enhances both the efficiency of refolding and correct disulfide formation.
abstract: Protein refolding constitutes a crucial process for recombinant proteins. We report here on the development of a multifunctional refolding additive, glutathione ethyl ester (GSHEE), prepared from a redox reagent glutathione and an amino acid ethyl ester, an aggregation suppressor. Compared to glutathione, GSHEE showed 3.2-fold higher efficiency for the refolding yield of hen egg lysozyme. More importantly, a low concentration of GSHEE is more effective for refolding than conventional additives, such as amino acid ethyl esters by two orders of magnitude. The high potency of GSHEE makes it a candidate for use as a refolding additive for use in conjunction with reduced and denatured proteins.
authors: Japan Synchrotron Radiation Research Institute-SPring-8, 1-1-1 Kouto, Sayo, 679-5198 Hyogo, Japan. l-ito@spring8.or.jp
authors: Len
authors: L
authors: Ito
authors: Masaki
authors: M
authors: Okumura
authors: Kohsaku
authors: K
authors: Tao
authors: Yusuke
authors: Y
authors: Kasai
authors: Shunsuke
authors: S
authors: Tomita
authors: Akiko
authors: A
authors: Oosuka
authors: Hidetoshi
authors: H
authors: Yamada
authors: Tomohisa
authors: T
authors: Shibano
authors: Kentaro
authors: K
authors: Shiraki
authors: Takashi
authors: T
authors: Kumasaka
authors: Hiroshi
authors: H
authors: Yamaguchi
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002021:Buffers; D002642:Chick Embryo; D003553:Cystine / Q000737:chemistry*; D005978:Glutathione / Q000031:analogs & derivatives* / Q000737:chemistry; D019803:Glutathione Disulfide / Q000737:chemistry; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry; D010084:Oxidation-Reduction; D058849:Protein Refolding; D012995:Solubility
chemical_list: D000596:Amino Acids; D002021:Buffers; D003553:Cystine; C042431:S-ethyl glutathione; D009113:Muramidase; D005978:Glutathione; D019803:Glutathione Disulfide