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Protein J. 2012 Aug;31(6):499-503. doi: 10.1007/s10930-012-9427-4.

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

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1
Japan Synchrotron Radiation Research Institute-SPring-8, 1-1-1 Kouto, Sayo, 679-5198 Hyogo, Japan. l-ito@spring8.or.jp

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.

PMID:
22752753
DOI:
10.1007/s10930-012-9427-4
[Indexed for MEDLINE]
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