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Glutathione Ethylester, a Novel Protein Refolding Reagent, Enhances both the Efficiency of Refolding and Correct Disulfide Formation |
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| Authors: | Len Ito Masaki Okumura Kohsaku Tao Yusuke Kasai Shunsuke Tomita Akiko Oosuka Hidetoshi Yamada Tomohisa Shibano Kentaro Shiraki Takashi Kumasaka Hiroshi Yamaguchi |
| Affiliation: | 1. Japan Synchrotron Radiation Research Institute (SPring-8), 1-1-1 Kouto, Sayo, 679-5198, Hyogo, Japan 2. School of Science and Technology, Kwansei Gakuin University, Sanda, 669-1337, Hyogo, Japan 3. Milbon Co., Ltd., 2-3-35 Zengenzi, Miyakozima, 534-0015, Osaka, Japan 4. Laboratory of Biostructural Chemistry, Graduate School of Life Sciences, Tohoku University, Sendai, 980-8577, Miyagi, Japan 5. Institute of Applied Physics, University of Tsukuba, Tsukuba, 305-8573, Ibaraki, Japan |
| 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. |
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