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http://dx.doi.org/10.5012/bkcs.2004.25.9.1366

Effect of Linker for Immobilization of Glutathione on BSA-Assembled Controlled Pore Glass Beads  

Chen, Li-Hua (Center for Integrated Molecular Systems, Department of Chemistry, Pohang University of Science and Technology, Institute of Functional Material Chemistry, Faculty of Chemistry, Northeast Normal University)
Choi, Young-Seo (Center for Integrated Molecular Systems, Department of Chemistry, Pohang University of Science and Technology)
Park, Jung-Won (Center for Integrated Molecular Systems, Department of Chemistry, Pohang University of Science and Technology)
Kwon, Joseph (Sigmol Incorporation)
Wang, Rong-Shun (Institute of Functional Material Chemistry, Faculty of Chemistry, Northeast Normal University)
Lee, Tae-Hoon (Sigmol Incorporation)
Ryu, Sung-Ho (Department of Life Science, Pohang University of Science and Technology)
Park, Joon-Won (Center for Integrated Molecular Systems, Department of Chemistry, Pohang University of Science and Technology)
Publication Information
Abstract
Controlled pore glass bead was modified with bovine serum albumin (BSA), and glutathione (GSH) was immobilized through three kinds of linkers on top of BSA. Bis(3-sulfo-N-hydroxysuccinimide suberate) sodium salt $(BS^3)$, N-hydroxysuccinimide 3-(2-pyridyldithio)propionate (SPDP), or N-hydroxysuccinimide 4-maleimidobutyrate (GMBS) was introduced into the BSA-bound matrix. Subsequently, GSH was immobilized by addition of thiol side chain into the maleimido moiety, replacing a disulfide group, or formation of an amide group upon releasing 3-sulfo-N-hydroxysuccimide group. It was observed that conjugation methodology played a critical role for activity of the immobilized GSH. SDS-PAGE chromatogram showed that the matrix of glutathione immobilized on BSA through GMBS manifested high selectivity towards glutathione-S-transferase (GST) in cell lysate.
Keywords
Glutathione (GSH); Glutathione-S-transferase (GST); Controlled pore glass (CPG); Linker; Bovine serum albumin (BSA);
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