Glutathione ethylester, a novel protein refolding reagent, enhances both the efficiency of refolding and correct disulfide formation

Len Ito, Masaki Kumura, Kohsaku Tao, Yusuke Kasai, Shunsuke Tomita, Akiko Oosuka, Hidetoshi Yamada, Tomohisa Shibano, Kentaro Shiraki, Takashi Kumasaka, Hiroshi Yamaguchi

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)499-503
Number of pages5
JournalProtein Journal
Volume31
Issue number6
DOIs
Publication statusPublished - 2012 Aug 1
Externally publishedYes

Keywords

  • Aggregation
  • Glutathione
  • Glutathione ethyl ester
  • Redox
  • Refolding

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Organic Chemistry

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